Source 1primary paper2016Biochemistry
Toolkit/iLID N414L variant
iLID N414L variant
Also known as: N414L
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The iLID N414L variant is a modified iLID light-inducible dimerization system in which an N414L point mutation in the LOV domain lengthens the reversion half-life. In combination with SspB binding partners, it supports blue-light-dependent control of protein colocalization and has been used in reengineered iLID-SspB systems for processes including transmembrane protein localization.
Usefulness & Problems
Why this is useful
This variant is useful because it alters the temporal behavior of the iLID switch by prolonging the lit-state reversion kinetics. The associated iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 uM, addressing conditions where dark-state association can compromise optical control.
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
Problem solved
The tool helps solve the problem of insufficient kinetic tuning in light-inducible dimerization systems, specifically by lengthening iLID reversion half-life through the N414L LOV-domain mutation. In the broader reengineered iLID-SspB context, it addresses control of protein interactions at high effective concentrations and reduces limitations from excessive dark-state colocalization when paired with appropriate SspB variants.
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
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
recombinationInput: Light
Implementation Constraints
Implementation requires the iLID construct carrying the N414L point mutation in the LOV domain and a compatible SspB binding partner. The system is activated by blue light, and the cited engineering work focused on tuning iLID-SspB behavior for proteins at effective concentrations of 5-100 uM, including transmembrane protein colocalization in neurons.
The supplied evidence directly supports the kinetic effect of the N414L mutation but does not provide a quantitative reversion half-life value for this variant. It also does not isolate application-specific performance of N414L itself apart from the broader iLID-SspB engineering context, so validation for recombination or other target processes is not detailed here.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2020Figshare
Ranked Claims
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.
Approval Evidence
2 sources4 linked approval claimsfirst-pass slug ilid-n414l-variant
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Source:
with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID
Source:
kinetic tuningsupports
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
Source:
scope expansionsupports
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
Source:
kinetic tuningsupports
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.
Source:
scope expansionsupports
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.
Source:
Comparisons
Source-backed strengths
The defining engineered property supported by the evidence is a lengthened reversion half-life caused by the N414L mutation in the LOV domain. In the related tuned iLID-SspB system, the SspB A58V dimer variant enabled light-activated colocalization of transmembrane proteins in neurons, and this partner showed a 42-fold light-dependent affinity change from 3 ± 2 uM to 125 ± 40 nM.
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).
Ranked Citations
- 1.
- 2.