Celastrol Inhibits Hsp90 Chaperoning of Steroid Receptors by Inducing Fibrillization of the Co-chaperone p23

Hsp90 is an ATP-dependent molecular chaperone. The best characterized inhibitors of Hsp90 target its ATP binding pocket, causing nonselective degradation of Hsp90 client proteins. Here, we show that the small molecule celastrol inhibits the Hsp90 chaperoning machinery by inactivating the co-chaperon...

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Bibliographic Details
Main Authors: Chadli, Ahmed, Felts, Sara J., Wang, Qin, Sullivan, William P., Botuyan, Maria Victoria, Fauq, Abdul, Ramirez-Alvarado, Marina, Mer, Georges
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2010
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2823561/
https://ncbi.nlm.nih.gov/pubmed/19996313
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.081018
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