1wa9
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(New page: 200px<br /><applet load="1wa9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wa9, resolution 3.15Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 03:09, 21 November 2007
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CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD
Overview
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.
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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