Structure of an Hsp90-Cdc37-Cdk4 complex

Vaughan, Cara K, Gohlke, Ulrich, Sobott, Frank, Good, Valerie M, Ali, Maruf M U, Prodromou, Chrisostomos, Robinson, Carol V, Saibil, Helen R and Pearl, Laurence H (2006) Structure of an Hsp90-Cdc37-Cdk4 complex. Molecular Cell, 23 (5). pp. 697-707. ISSN 1097-2765

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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.

Item Type: Article
Keywords: Cell Cycle Proteins/*chemistry/isolation & purification/*ultrastructure Chaperonins/*chemistry/isolation & purification/*ultrastructure Cyclin-Dependent Kinase 4/*chemistry/isolation & purification/*ultrastructure HSP90 Heat-Shock Proteins/*chemistry/isolation & purification/*ultrastructure Humans Microscopy, Electron Models, Molecular Multiprotein Complexes/chemistry/isolation & purification/ultrastructure Protein Binding
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science > QD Chemistry > QD0901 Crystallography
Depositing User: Chrisostomos Prodromou
Date Deposited: 24 Feb 2015 15:22
Last Modified: 02 Jul 2019 21:21

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