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Updated: Jul 11, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Structure of an Hsp90-Cdc37-Cdk4 complex.

Cara K Vaughan1, Ulrich Gohlke, Frank Sobott

  • 1Section of Structural Biology, The Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, UK.

Molecular Cell
|September 5, 2006
PubMed
Summary

The Hsp90 chaperone system and its adaptor Cdc37 bind protein kinases like Cdk4. Researchers determined the 3D structure of this complex, revealing how Cdk4 is recruited and regulated by Hsp90.

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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Area of Science:

  • Molecular Chaperones
  • Protein Kinase Regulation
  • Structural Biology

Background:

  • Protein kinase activation frequently relies on the Hsp90 molecular chaperone system.
  • The cochaperone adaptor protein Cdc37 bridges protein kinases and Hsp90, facilitating client recruitment.
  • Understanding the structural basis of this interaction is crucial for deciphering kinase regulation.

Purpose of the Study:

  • To express and purify a functional Hsp90-Cdc37-Cdk4 complex.
  • To determine the 3D structure of the Hsp90-Cdc37-Cdk4 complex using single-particle electron microscopy.
  • To elucidate the mechanism of protein kinase recruitment and regulation by the Hsp90 chaperone system.

Main Methods:

  • Protein expression and purification of the Hsp90-Cdc37-Cdk4 complex.
  • Single-particle electron microscopy for 3D structure determination.
  • Comparative structural analysis with existing Hsp90 crystal structures.

Main Results:

  • Successful expression and purification of the Hsp90-Cdc37-Cdk4 complex.
  • Determination of the complex's stoichiometry and 3D structure.
  • Identification of Cdc37 and Cdk4 binding sites within the Hsp90 complex.
  • Insights into the coupling mechanism between kinase conformational changes and the Hsp90 ATPase cycle.

Conclusions:

  • The study provides the first structural view of the Hsp90-Cdc37-Cdk4 complex.
  • Structural data reveals how Cdc37 acts as a scaffold to recruit Cdk4 to Hsp90.
  • The findings suggest a model for how Hsp90's ATPase cycle influences kinase conformation and activity.