Hsp90

Hsp90 (Heat Shock Protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are being studied as a treatment for cancer.

Structure

Hsp90 is a flexible and dynamic protein. It is composed of three different domains: the N-terminal domain, the middle domain, and the C-terminal domain. The N-terminal domain has ATP binding properties, the middle domain is necessary for client protein and co-chaperone binding, and the C-terminal domain involves dimerization.

Function

Hsp90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including kinases and transcription factors. It is also involved in protein degradation and is necessary for the proper functioning of the proteasome, a major protein degradation pathway in the cell.

Clinical significance

Hsp90 is often overexpressed in cancer cells, and its inhibition can affect multiple signaling pathways simultaneously. This makes it a promising target for new anti-cancer drugs. Several Hsp90 inhibitors are currently being tested in clinical trials.

See also

• Heat shock protein
• Chaperone (protein)
• Proteasome
• Cancer

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  Hsp90 schematic
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  Hsp90 ATP pocket
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  Hsp90 pincer movement
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  Hsp90 cycle
• Hsp90
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• Hsp90
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  GR Hsp90 translocation
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  Hsp90 cycle SHR