2cg9
From Proteopedia
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CRYSTAL STRUCTURE OF AN HSP90-SBA1 CLOSED CHAPERONE COMPLEX
Overview
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, ... [(full description)]
About this Structure
2CG9 is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae] with ATP as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex., Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH, Nature. 2006 Apr 20;440(7087):1013-7. PMID:16625188
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