Inhibiting Hsp90 has the potential to affect all the hallmarks of cancer, making it an exciting potential therapeutic target. HSP90 inhibitors that bind the ATP binding pocket standing on the N-terminal of HSP90 have resulted in degradation of HSP90 client proteins through the ubiquitin proteasome pathway. The natural product of HSP90 inhibitors geldanamycin and radicicol can exert their antitumor function by blocking the intrinsic ATPase activity of HSP90, leading to degradation of HSP90 client proteins. Thus, HSP90 inhibition provides an important pharmacological platform for anticancer therapy.

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