Source 1primary paper2009PLoS Biology
Toolkit/Drosophila PERIOD PAS-B beta-sheet surface
Drosophila PERIOD PAS-B beta-sheet surface
Also known as: dPER PAS-B beta-sheet surface
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Drosophila PERIOD PAS-B beta-sheet surface is a protein interaction interface within dPER that mediates binding to the clock protein TIMELESS (dTIM). Comparative analysis further indicates that this PAS-B beta-sheet surface is a reusable interaction site within PERIOD-family proteins, supporting dPER-dTIM heterodimer formation in Drosophila and mPER2 homodimerization in mammals.
Usefulness & Problems
Why this is useful
This interface is useful as a defined molecular determinant for studying circadian clock protein complex assembly in Drosophila. It also provides a comparative structural handle for analyzing how related PERIOD-family PAS domains deploy a conserved surface for distinct binding partners across species.
Problem solved
It helps identify the specific dPER surface that mediates interaction with dTIM, addressing the problem of mapping clock protein interaction determinants within PERIOD PAS domains. The comparative study also clarifies that analogous PAS-B beta-sheet surfaces can support different interaction modes in different PERIOD proteins.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
This tool is an interaction surface within the dPER PAS-B domain rather than a standalone effector domain. The supplied evidence does not specify construct boundaries, expression systems, cofactors, or delivery methods, beyond its role in mediating dPER interaction with dTIM.
The evidence provided comes from a single cited study and specifically supports interaction with dTIM, with limited detail here on mutational scope, binding affinity, or in vivo performance. No implementation data are provided for using this interface as an engineered module outside its native circadian protein 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 source2 linked approval claimsfirst-pass slug drosophila-period-pas-b-beta-sheet-surface
the PAS-B beta-sheet surface of dPER mediates interactions with TIMELESS (dTIM)
Source:
interaction mediationsupports
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)
Source:
interaction site rolesupports
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
Source:
Comparisons
Source-backed strengths
The interaction role is supported by structural and functional analyses reported for dPER PAS domain interactions. The same study places the dPER PAS-B beta-sheet surface in a broader comparative framework by contrasting it with mPER2, where the corresponding site mediates homodimerization rather than dTIM binding.
Source:
Our study reveals quantitative and qualitative differences between the homodimeric PAS domain interactions of dPER and its mammalian homologue mPER2.
Ranked Citations
- 1.