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Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural

Lorenzo I Finci1, Mayukh Chakrabarti1, Gulcin Gulten1

  • 1NCI RAS Initiative, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.

Communications Biology
|March 2, 2024
PubMed
Summary

The heat shock protein 90 (HSP90) chaperone complex, with cochaperone CDC37, facilitates the folding of RAF1 kinase. Cryo-EM structures reveal how HSP90 and CDC37 interact with RAF1 to guide its proper molecular assembly.

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