1fpz
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(New page: 200px<br /> <applet load="1fpz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpz, resolution 2.0Å" /> '''CRYSTAL STRUCTURE AN...)
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Revision as of 14:49, 12 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE
Overview
The CDK-interacting protein phosphatase KAP dephosphorylates, phosphoThr-160 (pThr-160) of the CDK2 activation segment, the site of, regulatory phosphorylation that is essential for kinase activity. Here we, describe the crystal structure of KAP in association with pThr-160-CDK2, representing an example of a protein phosphatase in complex with its, intact protein substrate. The major protein interface between the two, molecules is formed by the C-terminal lobe of CDK2 and the C-terminal, helix of KAP, regions remote from the kinase-activation segment and the, KAP catalytic site. The kinase-activation segment interacts with the, catalytic site of KAP almost entirely via the phosphate group of pThr-160., This interaction requires that the activation segment is unfolded and, drawn away from the kinase molecule, inducing a conformation of CDK2, similar to the activated state observed in the CDK2/cyclin A complex.
About this Structure
1FPZ is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2., Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D, Mol Cell. 2001 Mar;7(3):615-26. PMID:11463386
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