Source 1primary paper2026MED
Toolkit/NpF2164g6
NpF2164g6
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
NpF2164g6 is a 17 kDa cyanobacteriochrome GAF domain used in the UNICYCL red-light-responsive protein interaction system. In this system, it forms a 1:1 complex with the 6 kDa binder BNp-Red-1.2 in the dark with an approximately 1–5 μM dissociation constant.
Usefulness & Problems
Why this is useful
NpF2164g6 is useful as the photosensory domain in a compact red-light-regulated protein interaction system. The source positions UNICYCL as smaller and simpler than phytochrome-based systems, supporting its use where reduced tool size and architectural simplicity are advantageous.
Source:
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
Problem solved
NpF2164g6 helps address the need for a red-light-responsive protein interaction module that is more compact than phytochrome-based alternatives. The supplied evidence supports its role in dark-state complex formation with BNp-Red-1.2, but does not provide direct application data beyond this positioning.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
dark-state complex formationlight-regulated protein-protein bindingthermal dark-state reversionTechniques
Structural CharacterizationTarget processes
recombinationInput: Light
Implementation Constraints
NpF2164g6 is implemented as a protein domain within the UNICYCL system and pairs with the 6 kDa binder BNp-Red-1.2. The available evidence does not specify construct architecture, chromophore requirements, expression context, or delivery considerations.
The supplied evidence is limited to one source and provides only binding stoichiometry, approximate affinity, and comparative positioning. No independent replication, organism-specific validation, wavelength-specific performance, or recombination assay data are provided in the evidence set.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
dissociation constant ≈ 1-5 μMstoichiometry 1:1 complex
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
UNICYCL is positioned as a smaller and simpler red-light tool than phytochrome-based systems.
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
dark state reversion half life ∼ 1 min
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
binding affinity change 25
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
UNICYCL is a small red-light-only optogenetic system for controlling protein-protein interactions.
This system provides a small, simple red-light-only optogenetic tool that can operate to control protein-protein interactions in vitro and in living cells.
Approval Evidence
1 source4 linked approval claimsfirst-pass slug npf2164g6
BNp-Red-1.2 (6 kDa) binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark. The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
Source:
binding behaviorsupports
BNp-Red-1.2 binds NpF2164g6 in the dark with approximately 1-5 μM dissociation constant to form a 1:1 complex.
BNp-Red-1.2 (6 kDa) that binds to a cyanobacteriochrome (CBCR) GAF domain NpF2164g6 (17 kDa) with a Kd ≈ 1-5 μM to form a 1:1 complex in the dark.
Source:
kinetic propertysupports
NpF2164g6 reverts to the dark state with an approximately 1 minute half-life and the complex reforms.
The CBCR GAF domain reverts to the dark state with a half-life of ∼ 1 min and the complex reforms.
Source:
light responsesupports
Red light dissociates the BNp-Red-1.2 and NpF2164g6 complex by decreasing binding affinity more than 25-fold.
Red light causes dissociation of the complex by causing a > 25-fold decrease in binding affinity.
Source:
mechanistic insightsupports
Structural analysis indicates that BNp-Red-1.2 interacts with the GAF domain and senses bilin chromophore isomerization at a site overlapping the critical phytochrome tongue domain region.
Structural analysis using NMR measurements combined with molecular docking and dynamics simulations shows that the binder interacts with the GAF domain and senses isomerization of the bilin chromophore at a site that overlaps the critical tongue domain of phytochromes.
Source:
Comparisons
Source-backed strengths
The domain supports defined 1:1 binding to BNp-Red-1.2 with an approximately 1–5 μM dissociation constant in the dark. Its small size as a 17 kDa GAF domain contributes to the reported smaller and simpler overall UNICYCL system relative to phytochrome-based tools.
Source:
Current red-light tools are primarily based on phytochromes, large dimeric proteins with a structurally complex mode of interaction with their binding partners. Here we introduce a small red-light-only responsive system...
Ranked Citations
- 1.