1fq1

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{{STRUCTURE_1fq1| PDB=1fq1 | SCENE= }}
{{STRUCTURE_1fq1| PDB=1fq1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2'''
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===CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11463386 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11463386}}
==About this Structure==
==About this Structure==
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[[Category: Song, H.]]
[[Category: Song, H.]]
[[Category: Phospho-protein/protein complex]]
[[Category: Phospho-protein/protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:45:57 2008''

Revision as of 00:46, 1 July 2008

Image:1fq1.png

Template:STRUCTURE 1fq1

CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2

Template:ABSTRACT PUBMED 11463386

About this Structure

1FQ1 is a Protein complex structure of sequences from Homo sapiens. 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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