1usu: Difference between revisions
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Revision as of 17:05, 30 October 2007
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THE STRUCTURE OF THE COMPLEX BETWEEN AHA1 AND HSP90
OverviewOverview
Hsp90 is a molecular chaperone essential for the activation and assembly, of many key eukaryotic signalling and regulatory proteins. Hsp90 is, assisted and regulated by co-chaperones that participate in an ordered, series of dynamic multiprotein complexes, linked to Hsp90 conformationally, coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and, stimulate its ATPase activity. Biochemical analysis shows that this, activity is dependent on the N-terminal domain of Aha1, which interacts, with the central segment of Hsp90. The structural basis for this, interaction is revealed by the crystal structure of the N-terminal domain, (1-153) of Aha1 (equivalent to the whole of Hch1) in complex with the, middle segment of Hsp90 (273-530). Structural analysis and mutagenesis, show that ... [(full description)]
About this StructureAbout this Structure
1USU is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae] with GOL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery., Meyer P, Prodromou C, Liao C, Hu B, Roe SM, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH, EMBO J. 2004 Mar 24;23(6):1402-10. PMID:15039704
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