1c25: Difference between revisions

Revision as of 20:06, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1c25.png

Template:STRUCTURE 1c25

HUMAN CDC25A CATALYTIC DOMAINHUMAN CDC25A CATALYTIC DOMAIN

Template:ABSTRACT PUBMED 9604936

About this StructureAbout this Structure

1C25 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A., Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, Piwnica-Worms H, Rink MJ, Saper MA, Cell. 1998 May 15;93(4):617-25. PMID:9604936

Page seeded by OCA on Mon Jun 30 20:06:21 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1c25.gif|left|200px]]
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-'''HUMAN CDC25A CATALYTIC DOMAIN'''
+===HUMAN CDC25A CATALYTIC DOMAIN===
-==Overview==
+<!--
-Cdc25 phosphatases activate the cell division kinases throughout the cell cycle. The 2.3 A structure of the human Cdc25A catalytic domain reveals a small alpha/beta domain with a fold unlike previously described phosphatase structures but identical to rhodanese, a sulfur-transfer protein. Only the active-site loop, containing the Cys-(X)5-Arg motif, shows similarity to the tyrosine phosphatases. In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress. Asp-383, previously proposed to be the general acid, instead serves a structural role, forming a conserved buried salt-bridge. We propose that Glu-431 may act as a general acid. Structure-based alignments suggest that the noncatalytic domain of the MAP kinase phosphatases will share this topology, as will ACR2, a eukaryotic arsenical resistance protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_9604936}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9604936 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9604936}}
 ==About this Structure==
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 [[Category: Cell cycle phosphatase,dual specificity protein phosphatase]]
 [[Category: Hydrolase]]
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