1fpz
From Proteopedia
(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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caption="1fpz, resolution 2.0Å" /> | caption="1fpz, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FPZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1FPZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FPZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha-beta sandwich]] | [[Category: alpha-beta sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:47 2008'' |
Revision as of 13:48, 15 February 2008
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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 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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