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Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.

Abstract：

:The molecular chaperone Hsp90 is essential for the correct folding, maturation and activation of a diverse array of client proteins, including several key constituents of oncogenic processes. Hsp90 has become a focus of cancer research, since it represents a target for direct prophylaxis against multistep malignancy. Hydrogen-exchange mass spectrometry was used to study the structural and conformational changes undergone by full-length human Hsp90beta in solution upon binding of the kinase-specific co-chaperone Cdc37 and two Hsp90 ATPase inhibitors: Radicicol and the first-generation anticancer drug DMAG. Changes in hydrogen exchange pattern in the complexes in regions of Hsp90 remote to the ligand-binding site were observed indicating long-range effects. In particular, the interface between the N-terminal domain and middle domains exhibited significant differences between the apo and complexed forms. For the inhibitors, differences in the interface between the middle domain and the C-terminal domain were also observed. These data provide important insight into the structure of the biologically active form of the protein.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Phillips JJ,Yao ZP,Zhang W,McLaughlin S,Laue ED,Robinson CV,Jackson SE

doi

10.1016/j.jmb.2007.04.059

subject

Has Abstract

pub_date

2007-10-05 00:00:00

pages

1189-203

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)00559-1

journal_volume

372

pub_type

杂志文章

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