Source 1review2024ACS Synthetic Biology
Toolkit/SspB
SspB
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Assembly Hierarchy
Part of
- iLID/SspBmulti component switch← this item is a component
Summary
SspB is the binding partner used in the iLID blue-light-inducible dimerization system. Upon blue-light activation of iLID, the exposed SsrA peptide binds SspB, enabling light-controlled recruitment and localization of SspB-fused cargo proteins.
Usefulness & Problems
Why this is useful
SspB is useful as a recruitable protein domain for optogenetic control of protein localization in the iLID system. Reported work also shows that SspB recruitment remains effective when iLID is targeted to GFP-tagged proteins through an antiGFP nanobody, increasing targeting flexibility without engineering the target protein itself.
Source:
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
Source:
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
Source:
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
Source:
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
Problem solved
SspB helps solve the problem of achieving reversible, light-dependent recruitment of proteins to defined cellular locations. In the antiGFP-nanobody implementation, it also addresses the need to target iLID to existing GFP-tagged proteins without direct fusion of iLID to each target.
Source:
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
Source:
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
Source:
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
localizationrecombinationInput: Light
Implementation Constraints
SspB is implemented as one of the two components of the iLID system and is used as a fusion partner to recruit cargo after blue-light activation of iLID. Practical evidence also supports pairing iLID with an antiGFP nanobody to target GFP-tagged proteins, while SspB serves as the recruited binding partner for the light-exposed SsrA peptide.
The provided evidence is focused on SspB as a component of the iLID system and does not report standalone performance metrics for SspB such as affinity values, kinetics, dynamic range, or organism-specific validation. Evidence for applications beyond localization, including recombination, is not directly supported by the supplied text.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2014Proceedings of the National Academy of Sciences
Source 3review2024Frontiers in Physiology
Source 4primary paper2016Biochemistry
Source 5primary paper2020Figshare
Source 6primary paper2022
Ranked Claims
Genetically encoded biosensors and optogenetic tools have been developed to study dynamic T cell signaling pathways in live cells.
Therefore, genetically encoded biosensors and optogenetic tools have been developed to study dynamic T cell signaling pathways in live cells.
The reviewed optical tools have been primarily applied to dynamic molecular events in TCR signaling and may aid understanding of CAR activation and function.
They have been primarily applied to the study of dynamic molecular events in TCR signaling, and they will further aid in understanding the mechanisms of CAR activation and function.
These optical technologies revealed dynamic and complex molecular mechanisms at each stage of T cell signaling pathways.
We review these cutting-edge technologies that revealed dynamic and complex molecular mechanisms at each stage of T cell signaling pathways.
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
higher affinity switch range 0.8-47 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity fold change 42binding affinity state 1 3 b1 2 bcMbinding affinity state 2 125 b1 40 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
effective protein concentration range 5-100 bcM
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.
allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark
comparison switch affinity range 0.8-47 bcM
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.
The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)
binding affinity 3 bcMbinding affinity 125 bcMfold change in binding affinity 42
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
effective protein concentration range 5-100 bcM
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.
Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.
This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was functionally demonstrated through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
We demonstrate the functional utility of the switch through light-mediated subcellular localization in mammalian cell culture and reversible control of small GTPase signaling.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
The switch was created by embedding the bacterial SsrA peptide in the C-terminal helix of the Avena sativa LOV2 domain.
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
change in binding affinity for SspB with light stimulation twofold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
change in affinity for SspB with light stimulation 50 fold
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
A crystal structure of iLID shows a critical interaction between the LOV2 surface and an engineered phenylalanine that more tightly pins the SsrA peptide against LOV2 in the dark.
A crystal structure of iLID shows a critical interaction between the surface of the LOV2 domain and a phenylalanine engineered to more tightly pin the SsrA peptide against the LOV2 domain in the dark.
Approval Evidence
6 sources9 linked approval claimsfirst-pass slug sspb
Explicitly supported tool/component names recovered from sources include optoDroplets, Corelets, OptoGranules, Cry2, iLID, SspB, ferritin/FTH1, G3BP1, and MBP-based OptoMBP.
Source:
The strongest explicit tool/component names supported by discovered sources are LiCAR, OptoCAR, iLID, SspB, cpLOV2, and granzyme-B FRET reporter / FRET-shift screening.
Source:
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
Source:
its binding partner SspB
Source:
iLID, and its binding partner SspB
Source:
allowing the SsrA peptide to bind SspB
Source:
functional compatibilitysupports
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
Source:
mechanismsupports
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
Source:
engineering resultsupports
The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
Source:
mechanismsupports
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB
Source:
engineering resultsupports
The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
Source:
mechanismsupports
iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.
iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.
Source:
mechanismsupports
In the dark, the SsrA peptide is sterically blocked from binding SspB, and blue-light activation allows binding by undocking the LOV2 C-terminal helix.
In the dark the SsrA peptide is sterically blocked from binding its natural binding partner, SspB. When activated with blue light, the C-terminal helix of the LOV2 domain undocks from the protein, allowing the SsrA peptide to bind SspB.
Source:
performancesupports
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Source:
performance improvementsupports
The improved light inducible dimer iLID changes its affinity for SspB by over 50-fold with light stimulation.
create an improved light inducible dimer (iLID) that changes its affinity for SspB by over 50-fold with light stimulation
Source:
Comparisons
Source-backed strengths
The supplied evidence supports efficient blue-light-dependent heterodimerization between iLID and SspB and efficient recruitment in an iLID-antiGFP-nanobody configuration. The cited literature base includes the original iLID report and later work on tuning binding affinities and reversion kinetics, indicating that the iLID-SspB interaction has been engineered and reused across studies.
Source:
we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)
Source:
Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).
Source:
To create a switch that meets these criteria we have embedded the bacterial SsrA peptide in the C-terminal helix of a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain from Avena sativa.
Source:
Without optimization, the switch exhibited a twofold change in binding affinity for SspB with light stimulation.
Ranked Citations
- 1.
Extracted from this source document.
- 2.
- 3.
- 4.
- 5.
- 6.