Source 1primary paper2012The Journal of Chemical Physics
Toolkit/AsLOV2-Jα
AsLOV2-Jα
Also known as: AsLOV2-Jα domain, LOV-2-Jα photoswitch of phototropin1 from Avena sativa, photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
AsLOV2-Jα is the light-oxygen-voltage-2/Jα photoswitch domain from Avena sativa phototropin1. In the reported LOV-TAP fusion, ligation of AsLOV2-Jα to TrpR enables light-dependent control of DNA binding through photoinduced structural and electrostatic changes.
Usefulness & Problems
Why this is useful
AsLOV2-Jα is useful as a modular light-responsive domain for engineering allosteric control into fusion proteins. In the cited LOV-TAP system, it provides optical regulation of DNA association by coupling photoactivation to changes in Jα-helix docking, interdomain flexibility, and DNA-surface electrostatics.
Source:
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
Problem solved
This domain helps solve the problem of imposing reversible light control over protein-DNA interactions in an engineered signaling construct. The cited work specifically addresses how a photosensory module can be fused to TrpR to switch DNA binding through allosteric transduction.
Problem links
Need conditional control of signaling activity
DerivedAsLOV2-Jα is the LOV2-Jα photoswitch domain from Avena sativa phototropin1. In the cited LOV-TAP construct, this domain confers light-dependent control of DNA binding by undergoing photoinduced structural changes that alter electrostatic interactions with DNA.
Need precise spatiotemporal control with light input
DerivedAsLOV2-Jα is the LOV2-Jα photoswitch domain from Avena sativa phototropin1. In the cited LOV-TAP construct, this domain confers light-dependent control of DNA binding by undergoing photoinduced structural changes that alter electrostatic interactions with DNA.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
allosteric switchingallosteric switchingelectrostatic modulation of dna bindingelectrostatic modulation of dna bindinglight-induced conformational unfolding and flexibilizationlight-induced conformational unfolding and flexibilizationlight-triggered jα-helix undocking/cleavage from the lov corelight-triggered jα-helix undocking/cleavage from the lov corePhotocleavagephotoinduced cysteinyl-flavin adduct formationphotoinduced cysteinyl-flavin adduct formationTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: cleavageswitch architecture: uncaging
The cited implementation uses AsLOV2-Jα as a fusion partner ligated to TrpR in the artificial LOV-TAP construct. Mechanistic operation depends on the LOV-domain FMN chromophore and photoinduced formation of a Cys450-FMN adduct; beyond this, the supplied evidence does not provide expression, delivery, or construct-optimization details.
The evidence provided is narrow and comes from a 2012 computer simulation study rather than broad experimental validation. Reported function is specific to the LOV-TAP fusion with TrpR, and the supplied sources do not establish general performance, kinetics, wavelength dependence, or independent replication across other constructs or organisms.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2012Proteins Structure Function and Bioinformatics
Ranked Claims
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
Unfolding and flexibilization of the interdomain hairpin-like helix-loop-helix region enables condensation of LOV-TAP onto the DNA surface.
This goes along with the flexibilization through unfolding of a hairpin-like helix-loop-helix region interlinking the AsLOV2-Jα- and TrpR-domains, ultimately enabling the condensation of LOV-TAP onto the DNA surface.
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
In PA-Rac1, detachment of the peripheral alpha-helix induces release of the AsLOV2 inhibitor from the switchII activation site of the GTPase, enabling signal activation through effector-protein binding.
In the case of the PA-Rac1 system we find that this latter process induces the release of the AsLOV2-inhibitor from the switchII-activation site of the GTPase, enabling signal activation through effector-protein binding
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
Approval Evidence
2 sources6 linked approval claimsfirst-pass slug aslov2-j
the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα)
Source:
the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα)
Source:
compositionsupports
LOV-TAP is an artificial protein construct in which AsLOV2-Jα is ligated to TrpR.
the artificial protein construct light-oxygen-voltage (LOV)-tryptophan-activated protein (TAP), in which the LOV-2-Jα photoswitch of phototropin1 from Avena sativa (AsLOV2-Jα) has been ligated to the tryptophan-repressor (TrpR) protein from Escherichia coli
Source:
mechanismsupports
After photoexcitation, Cys450-FMN adduct formation in the AsLOV2-Jα binding pocket induces cleavage of the peripheral Jα-helix from the LOV core.
Cys450-FMN-adduct formation in the AsLOV2-Jα-binding pocket after photoexcitation induces the cleavage of the peripheral Jα-helix from the LOV core
Source:
mechanismsupports
In the dark state, the AsLOV2-Jα photoswitch exerts a repulsive electrostatic force on the DNA surface, leading to distortion of the hairpin region and disruption of LOV-TAP from DNA.
in the dark state the AsLOV2-Jα photoswitch remains inactive and exerts a repulsive electrostatic force on the DNA surface. This leads to a distortion of the hairpin region, which finally relieves its tension by causing the disruption of LOV-TAP from the DNA.
Source:
mechanismsupports
Light activation changes the polarity of the LOV photoswitch and promotes electrostatic attraction of LOV-TAP onto the DNA surface.
causing a change of its polarity and electrostatic attraction of the photoswitch onto the DNA surface
Source:
mechanistic pathwaysupports
The signaling pathway of AsLOV2-Jα begins with residual rearrangement and subsequent hydrogen-bond formation of amino acids near the flavin-mononucleotide chromophore, causing coupling between beta-strands and subsequent detachment of a peripheral alpha-helix from the AsLOV2 domain.
their signaling pathways begin with a residual re-arrangement and subsequent H-bond formation of amino acids near to the flavin-mononucleotide chromophore, causing a coupling between β-strands and subsequent detachment of a peripheral α-helix from the AsLOV2-domain
Source:
method capabilitysupports
The multiscale-modeling method is suitable for investigating the signaling behavior of AsLOV2-Jα and PA-Rac1.
we present in this paper a novel multiscale-modeling method, based on a combination of the kinetic Monte-Carlo- and MD-technique, and demonstrate its suitability for investigating the signaling behavior of the photoswitch light-oxygen-voltage-2-Jα domain from Avena Sativa (AsLOV2-Jα) and an AsLOV2-Jα-regulated photoactivable Rac1-GTPase (PA-Rac1)
Source:
Comparisons
Source-backed strengths
The available evidence supports a mechanistically explicit model in which photoexcitation drives Cys450-FMN adduct formation, Jα-helix cleavage/undocking from the LOV core, and subsequent electrostatic attraction to DNA. The study also identifies unfolding and flexibilization of a hairpin-like helix-loop-helix region as a structural basis for condensation of LOV-TAP onto the DNA surface.
Compared with light-harvesting complex II
AsLOV2-Jα and light-harvesting complex II address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: photocleavage; same primary input modality: light
Relative tradeoffs: appears more independently replicated.
AsLOV2-Jα and photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA) address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: allosteric switching; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with uniRapR module
AsLOV2-Jα and uniRapR module address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: allosteric switching; same primary input modality: light
Strengths here: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
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