1fq1: Difference between revisions
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[[Image:1fq1.jpg|left|200px]] | [[Image:1fq1.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2''' | {{Structure | ||
|PDB= 1fq1 |SIZE=350|CAPTION= <scene name='initialview01'>1fq1</scene>, resolution 3.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FQ1 is a [ | 1FQ1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ1 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11463386 11463386] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: phospho-protein/protein complex]] | [[Category: phospho-protein/protein complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:27 2008'' | ||
Revision as of 09:12, 20 March 2008
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| 1fq1, resolution 3.0Å | |||||||||||||
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| Ligands: | MG and ATP | ||||||||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2
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
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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