CDC37
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| Cdc37 N terminal kinase binding | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | CDC37_N | ||||||||
| Pfam | PF03234 | ||||||||
| InterPro | IPR013855 | ||||||||
| SCOP | 1us7 | ||||||||
| SUPERFAMILY | 1us7 | ||||||||
|
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| Cdc37 Hsp90 binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1us7 EBI.jpg
complex of hsp90 and p50
|
|||||||||
| Identifiers | |||||||||
| Symbol | CDC37_M | ||||||||
| Pfam | PF08565 | ||||||||
| InterPro | IPR013874 | ||||||||
| SCOP | 1us7 | ||||||||
| SUPERFAMILY | 1us7 | ||||||||
|
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| Cdc37 C terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1us7 EBI.jpg
complex of hsp90 and p50
|
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| Identifiers | |||||||||
| Symbol | CDC37_C | ||||||||
| Pfam | PF08564 | ||||||||
| InterPro | IPR013873 | ||||||||
| SCOP | 1us7 | ||||||||
| SUPERFAMILY | 1us7 | ||||||||
|
|||||||||
Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.[1][2]
The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a molecular 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.[3]
Interactions
CDC37 has been shown to interact with:
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Domain architecture
CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases.[11] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.[12] The function of the C-terminal domain is unclear.
References
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Further reading
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This article incorporates text from the public domain Pfam and InterPro IPR013855
This article incorporates text from the public domain Pfam and InterPro IPR013874
This article incorporates text from the public domain Pfam and InterPro IPR013873
