1fq1: Difference between revisions
New page: left|200px<br /> <applet load="1fq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fq1, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1fq1. | [[Image:1fq1.jpg|left|200px]]<br /><applet load="1fq1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1fq1, resolution 3.0Å" /> | caption="1fq1, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2'''<br /> | '''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1FQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http:// | 1FQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: phospho-protein/protein complex]] | [[Category: phospho-protein/protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:50 2008'' | ||
Revision as of 16:48, 15 February 2008
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CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2
OverviewOverview
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 StructureAbout this Structure
1FQ1 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
ReferenceReference
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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