Publication
Title
Structure of an Hsp90-Cdc37-Cdk4 complex
Author
Abstract
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.
Language
English
Source (journal)
Molecular cell. - Cambridge, Mass.
Publication
Cambridge, Mass. : 2006
ISSN
1097-2765
Volume/pages
23:5(2006), p. 697-707
ISI
000240663400008
Full text (Publisher's DOI)
UAntwerpen
Faculty/Department
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 30.06.2011
Last edited 06.06.2017