1wa9
From Proteopedia
(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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| - | [[Image:1wa9.gif|left|200px]]<br /><applet load="1wa9" size=" | + | [[Image:1wa9.gif|left|200px]]<br /><applet load="1wa9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wa9, resolution 3.15Å" /> | caption="1wa9, resolution 3.15Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD'''<br /> | '''CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PERIOD proteins are central components of the Drosophila and mammalian | + | 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== | ==About this Structure== | ||
| - | 1WA9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | + | 1WA9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polymorphism]] | [[Category: polymorphism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:08 2008'' |
Revision as of 13:42, 21 February 2008
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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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