1hk7

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{{STRUCTURE_1hk7| PDB=1hk7 | SCENE= }}
{{STRUCTURE_1hk7| PDB=1hk7 | SCENE= }}
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'''MIDDLE DOMAIN OF HSP90'''
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===MIDDLE DOMAIN OF HSP90===
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==Overview==
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Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains. The crystal structure of the middle segment of yeast Hsp90 reveals considerable evolutionary divergence from the equivalent regions of other GHKL protein family members such as MutL and GyrB, including an additional domain of new fold. Using the known structure of the N-terminal nucleotide binding domain, a model for the Hsp90 dimer has been constructed. From this structure, residues implicated in the ATPase-coupled conformational cycle and in interactions with client proteins and the activating cochaperone Aha1 have been identified, and their roles functionally characterized in vitro and in vivo.
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(as it appears on PubMed at http://www.pubmed.gov), where 12667448 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12667448}}
==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Heat shock protein]]
[[Category: Heat shock protein]]
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Revision as of 05:18, 1 July 2008

Image:1hk7.png

Template:STRUCTURE 1hk7

MIDDLE DOMAIN OF HSP90

Template:ABSTRACT PUBMED 12667448

About this Structure

1HK7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions., Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH, Mol Cell. 2003 Mar;11(3):647-58. PMID:12667448

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