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Structure of an Hsp90-Cdc37-Cdk4 complex

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posted on 2023-06-08, 14:44 authored by Cara K Vaughan, Ulrich Gohlke, Frank Sobott, Valerie M Good, Maruf M U Ali, Chrisostomos ProdromouChrisostomos Prodromou, Carol V Robinson, Helen R Saibil, Laurence PearlLaurence Pearl
Activation of many protein kinases depends on their interaction with the Hsp90 molecular chaperone system. Recruitment of protein kinase clients to the Hsp90 chaperone system is mediated by the cochaperone adaptor protein Cdc37, which acts as a scaffold, simultaneously binding protein kinases and Hsp90. We have now expressed and purified an Hsp90-Cdc37-Cdk4 complex, defined its stoichiometry, and determined its 3D structure by single-particle electron microscopy. Comparison with the crystal structure of Hsp90 allows us to identify the locations of Cdc37 and Cdk4 in the complex and suggests a mechanism by which conformational changes in the kinase are coupled to the Hsp90 ATPase cycle.

History

Publication status

  • Published

File Version

  • Published version

Journal

Molecular Cell

ISSN

1097-2765

Publisher

Elsevier

Issue

5

Volume

23

Page range

697-707

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2015-02-24

First Open Access (FOA) Date

2015-02-24

First Compliant Deposit (FCD) Date

2015-02-24