Structure and mechanism of the Hsp90 molecular chaperone machinery

Pearl, Laurence H and Prodromou, Chrisostomos (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annual Review of Biochemistry, 75. pp. 271-294. ISSN 0066-4154

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Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 has revealed a complex mechanism of ATPase-coupled conformational changes and interactions with cochaperone proteins, which facilitate activation of Hsp90's diverse "clientele." Despite recent progress, key aspects of the ATPase-coupled mechanism of Hsp90 remain controversial, and the nature of the changes, engendered by Hsp90 in client proteins, is largely unknown. Here, we discuss present knowledge of Hsp90 structure and function gleaned from crystallographic studies of individual domains and recent progress in obtaining a structure for the ATP-bound conformation of the intact dimeric chaperone. Additionally, we describe the roles of the plethora of cochaperones with which Hsp90 cooperates and growing insights into their biochemical mechanisms, which come from crystal structures of Hsp90 cochaperone complexes.

Item Type: Article
Keywords: Adenosine Triphosphatases/chemistry/genetics/metabolism Adenosine Triphosphate/metabolism Animals Binding Sites Dimerization Enzyme Activation Fungal Proteins/chemistry/genetics/metabolism *HSP90 Heat-Shock Proteins/chemistry/genetics/metabolism Humans Models, Molecular *Molecular Chaperones/chemistry/genetics/metabolism Multiprotein Complexes *Protein Structure, Quaternary *Protein Structure, Tertiary
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0241 Organic chemistry > QD0415 Biochemistry
Q Science > QD Chemistry > QD0901 Crystallography
Depositing User: Chrisostomos Prodromou
Date Deposited: 25 Feb 2015 08:39
Last Modified: 25 Feb 2015 08:48
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