Source 1primary paper2009PLoS Biology
Toolkit/Drosophila PERIOD PAS domain fragment
Drosophila PERIOD PAS domain fragment
Also known as: dPER fragment, dPER PAS-A/PAS-B fragment
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Drosophila PERIOD PAS domain fragment is a dPER protein segment comprising the PAS-A and PAS-B domains. Structural and functional analyses indicate that this fragment participates in PAS-mediated protein interactions, with the PAS-B beta-sheet surface mediating heterodimer formation with Drosophila TIMELESS (dTIM).
Usefulness & Problems
Why this is useful
This fragment is useful for dissecting interaction surfaces within the Drosophila circadian clock protein PERIOD. It provides a defined domain-level reagent for studying how PAS-domain interfaces contribute to dPER partner recognition, particularly interaction with dTIM.
Problem solved
It helps isolate the specific region of dPER responsible for PAS-mediated binding behavior. In particular, it addresses the problem of identifying which surface within the dPER PAS region mediates heterodimerization with dTIM.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Implementation Constraints
The construct is a Drosophila PERIOD fragment comprising two PER-ARNT-SIM domains, PAS-A and PAS-B. The supplied evidence does not report cofactors, host expression system, delivery modality, or specific construct boundaries beyond inclusion of the two PAS domains.
The available evidence is limited to one cited study and focuses on structural and functional analysis of interaction surfaces rather than broad tool validation. No evidence here describes expression conditions, binding affinities, in vivo performance, or use outside the reported dPER-dTIM interaction context.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface of dPER mediates interaction with TIMELESS (dTIM).
by yeast-two-hybrid experiments, that the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The PAS-B beta-sheet surface is a versatile interaction site that mediates mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system.
we identify the PAS-B beta-sheet surface as a versatile interaction site mediating mPER2 homodimerization in the mammalian system and dPER-dTIM heterodimer formation in the Drosophila system
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug drosophila-period-pas-domain-fragment
a Drosophila PERIOD (dPER) fragment comprising two PER-ARNT-SIM (PAS) domains (PAS-A and PAS-B)
Source:
comparative conclusionsupports
dPER and mPER2 have quantitative and qualitative differences in their homodimeric PAS domain interactions.
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
Source:
structural differencesupports
The mPER2 PAS domain fragment has a different dimer interface than dPER, stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419.
The mPER2 structure shows a different dimer interface than dPER, which is stabilized by interactions of the PAS-B beta-sheet surface including tryptophane 419
Source:
structural observationsupports
A dPER PAS domain fragment lacking the alphaF helix is monomeric.
Here we present the crystal structure of a monomeric PAS domain fragment of dPER lacking the alphaF helix.
Source:
Comparisons
Source-backed strengths
The fragment contains both PAS-A and PAS-B, the relevant interaction module analyzed in the cited study. Evidence specifically assigns the PAS-B beta-sheet surface as the interaction site for dTIM, and the work places this interface in a comparative context with mammalian PER2 PAS-domain interactions.
Source:
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
Ranked Citations
- 1.