Structure and in vivo function of Hsp90

Pearl, Laurence H and Prodromou, Chrisostomos (2000) Structure and in vivo function of Hsp90. Current Opinion in Structural Biology, 10 (1). pp. 46-51. ISSN 0959-440X

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Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.

Item Type: Article
Keywords: Adenosine Triphosphate/physiology Allosteric Regulation Animals Bacterial Proteins/chemistry/physiology Benzoquinones HSP90 Heat-Shock Proteins/antagonists & inhibitors/chemistry/*physiology Humans Lactams, Macrocyclic Macromolecular Substances Models, Biological Models, Molecular Protein Binding Quinones/pharmacology Signal Transduction/physiology Structure-Activity Relationship
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 07:45
Last Modified: 25 Feb 2015 07:45
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