Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene. This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.

01Interactions

CDC37 has been shown to interact with:

02Domain architecture

CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases. The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain. The function of the C-terminal domain is unclear.

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Sources and credits

This article is adapted from the Wikipedia article “CDC37”, written by its contributors and licensed under CC BY-SA 4.0. Fathomly has changed the layout, removed citation markers, navigation and maintenance notices, and adjusted punctuation. This adapted version is shared under the same license. For references, see the original article.

Images, from Wikimedia Commons:

Protein CDC37 PDB 1us7.png by Emw, CC BY-SA 3.0

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