1us7

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{{STRUCTURE_1us7| PDB=1us7 | SCENE= }}
{{STRUCTURE_1us7| PDB=1us7 | SCENE= }}
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'''COMPLEX OF HSP90 AND P50'''
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===COMPLEX OF HSP90 AND P50===
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==Overview==
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Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50(cdc37) acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via its C-terminal region. p50(cdc37) also has a regulatory activity, arresting Hsp90's ATPase cycle during client-protein loading. We have localized the binding site for p50(cdc37) to the N-terminal nucleotide binding domain of Hsp90 and determined the crystal structure of the Hsp90-p50(cdc37) core complex. Dimeric p50(cdc37) binds to surfaces of the Hsp90 N-domain implicated in ATP-dependent N-terminal dimerization and association with the middle segment of the chaperone. This interaction fixes the lid segment in an open conformation, inserts an arginine side chain into the ATP binding pocket to disable catalysis, and prevents trans-activating interaction of the N domains.
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(as it appears on PubMed at http://www.pubmed.gov), where 14718169 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14718169}}
==About this Structure==
==About this Structure==
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[[Category: Chaperone co-chaperone regulation]]
[[Category: Chaperone co-chaperone regulation]]
[[Category: Heat shock]]
[[Category: Heat shock]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:37:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:36:16 2008''

Revision as of 12:36, 27 July 2008

Image:1us7.png

Template:STRUCTURE 1us7

COMPLEX OF HSP90 AND P50

Template:ABSTRACT PUBMED 14718169

About this Structure

1US7 is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)., Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH, Cell. 2004 Jan 9;116(1):87-98. PMID:14718169

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