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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-8-15
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2-CDC28 Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/CDK2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CDKN3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin A,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Dual-Specificity Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphothreonine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
615-26
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11463386-Amino Acid Sequence,
pubmed-meshheading:11463386-Binding Sites,
pubmed-meshheading:11463386-CDC2-CDC28 Kinases,
pubmed-meshheading:11463386-Catalysis,
pubmed-meshheading:11463386-Crystallography, X-Ray,
pubmed-meshheading:11463386-Cyclin A,
pubmed-meshheading:11463386-Cyclin-Dependent Kinase 2,
pubmed-meshheading:11463386-Cyclin-Dependent Kinase Inhibitor Proteins,
pubmed-meshheading:11463386-Cyclin-Dependent Kinases,
pubmed-meshheading:11463386-Dual-Specificity Phosphatases,
pubmed-meshheading:11463386-Humans,
pubmed-meshheading:11463386-Models, Molecular,
pubmed-meshheading:11463386-Phosphoprotein Phosphatases,
pubmed-meshheading:11463386-Phosphoproteins,
pubmed-meshheading:11463386-Phosphorylation,
pubmed-meshheading:11463386-Phosphothreonine,
pubmed-meshheading:11463386-Protein Binding,
pubmed-meshheading:11463386-Protein Conformation,
pubmed-meshheading:11463386-Protein Tyrosine Phosphatase, Non-Receptor Type 1,
pubmed-meshheading:11463386-Protein Tyrosine Phosphatases,
pubmed-meshheading:11463386-Protein-Serine-Threonine Kinases
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pubmed:year |
2001
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pubmed:articleTitle |
Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2.
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pubmed:affiliation |
Department of Biochemistry, University of Oxford, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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