1wa9

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{{STRUCTURE_1wa9| PDB=1wa9 | SCENE= }}
{{STRUCTURE_1wa9| PDB=1wa9 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD'''
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===CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD===
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==Overview==
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PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.
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{{ABSTRACT_PUBMED_15629718}}
==About this Structure==
==About this Structure==
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[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
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Revision as of 12:03, 28 July 2008

Image:1wa9.png

Template:STRUCTURE 1wa9

CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD

Template:ABSTRACT PUBMED 15629718

About this Structure

1WA9 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD., Yildiz O, Doi M, Yujnovsky I, Cardone L, Berndt A, Hennig S, Schulze S, Urbanke C, Sassone-Corsi P, Wolf E, Mol Cell. 2005 Jan 7;17(1):69-82. PMID:15629718

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