Source 1primary paper2007Proceedings of the National Academy of Sciences
Toolkit/NC80 motif
NC80 motif
Also known as: NC80
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
NC80 is an 80-residue motif from Arabidopsis CRY2 that is sufficient to confer CRY2 physiological function. Source evidence indicates that blue light activates CRY2 by a phosphorylation-associated conformational change that derepresses the NC80 motif.
Usefulness & Problems
Why this is useful
NC80 provides a minimal CRY2-derived functional element for dissecting how cryptochrome photoactivation is encoded within a short sequence segment. Its activity in a GUS-NC80 fusion and its sufficiency for CRY2 physiological function make it useful for testing domain transfer and light-regulated derepression models.
Source:
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
Problem solved
This motif helps localize the functionally critical output region of Arabidopsis CRY2 to a defined 80-residue segment. It addresses the mechanistic problem of how blue light and CRY2 phosphorylation are linked to activation through derepression of a specific motif.
Problem links
Need precise spatiotemporal control with light input
DerivedNC80 is an 80-residue motif from Arabidopsis CRY2 that is sufficient to confer CRY2 physiological function. Source evidence indicates that blue light activates CRY2 by derepressing this motif through a phosphorylation-associated conformational change.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
conformational uncagingconformational uncagingConformational Uncagingphosphorylation-dependent derepressionphosphorylation-dependent derepressionTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatorswitch architecture: uncaging
The reported implementation involved a GUS-NC80 fusion protein expressed in transgenic plants. Blue light-induced CRY2 phosphorylation was implicated mechanistically, but the constitutively active GUS-NC80 fusion was described as unphosphorylated, indicating that motif exposure rather than phosphorylation of the isolated fusion correlated with activity.
Evidence is limited to a single cited study in Arabidopsis CRY2 and a GUS fusion context. The available evidence does not define transferability beyond the reported constructs, quantitative performance, or validation in non-plant systems.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated.
The GUS-NC80 fusion protein expressed in transgenic plants is constitutively active but unphosphorylated
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
The CRY2 C-terminal tail is required for blue light-induced CRY2 phosphorylation but not for CRY2 activity.
the CRY2 C-terminal tail was found to be required for the blue light-induced CRY2 phosphorylation but not for the CRY2 activity
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug nc80-motif
an 80-residue motif, referred to as NC80
Source:
functional sufficiencysupports
The 80-residue NC80 motif was sufficient to confer the physiological function of CRY2.
Our results showed that an 80-residue motif, referred to as NC80, was sufficient to confer the physiological function of CRY2.
Source:
mechanistic inferencesupports
Blue light-induced CRY2 phosphorylation likely causes a conformational change that derepresses the NC80 motif.
suggesting that the blue light-induced CRY2 phosphorylation causes a conformational change to derepress the NC80 motif
Source:
structural modelsupports
In unphosphorylated CRY2, the PHR domain and C-terminal tail form a closed conformation that suppresses the NC80 motif, whereas blue light-induced phosphorylation promotes an open conformation that derepresses NC80 and triggers signal transduction.
We propose that the PHR domain and the C-terminal tail of the unphosphorylated CRY2 form a "closed" conformation to suppress the NC80 motif in the absence of light. In response to blue light, the C-terminal tail of CRY2 is phosphorylated and electrostatically repelled from the surface of the PHR domain to form an "open" conformation, resulting in derepression of the NC80 motif and signal transduction to trigger photomorphogenic responses.
Source:
Comparisons
Source-backed strengths
The key strength is functional sufficiency: the 80-residue NC80 motif was reported to confer the physiological function of CRY2. In transgenic plants, a GUS-NC80 fusion was constitutively active despite being unphosphorylated, supporting the idea that exposure of this motif is sufficient for activity.
Compared with Avena sativa phototropin LOV2 domain
NC80 motif and Avena sativa phototropin LOV2 domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with Light-Oxygen-Voltage domain
NC80 motif and Light-Oxygen-Voltage domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Compared with photoswitchable inhibitory peptides
NC80 motif and photoswitchable inhibitory peptides address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: conformational uncaging, conformational_uncaging; same primary input modality: light
Ranked Citations
- 1.