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| [[Image:2cge.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2cge| PDB=2cge | SCENE= }} | | {{STRUCTURE_2cge| PDB=2cge | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF AN HSP90-SBA1 CLOSED CHAPERONE COMPLEX'''
| | ===CRYSTAL STRUCTURE OF AN HSP90-SBA1 CLOSED CHAPERONE COMPLEX=== |
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| ==Overview==
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| Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for the assembly and regulation of many eukaryotic signalling systems and is an emerging target for rational chemotherapy of many cancers. Although the structures of isolated domains of Hsp90 have been determined, the arrangement and ATP-dependent dynamics of these in the full Hsp90 dimer have been elusive and contentious. Here we present the crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1. The structure reveals the complex architecture of the 'closed' state of the Hsp90 chaperone, the extensive interactions between domains and between protein chains, the detailed conformational changes in the amino-terminal domain that accompany ATP binding, and the structural basis for stabilization of the closed state by p23/Sba1. Contrary to expectations, the closed Hsp90 would not enclose its client proteins but provides a bipartite binding surface whose formation and disruption are coupled to the chaperone ATPase cycle.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16625188}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16625188 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16625188}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hsp90]] | | [[Category: Hsp90]] |
| [[Category: Nucleotide-binding]] | | [[Category: Nucleotide-binding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:04:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:45:37 2008'' |
