Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

The molecular chaperone Hsp90 plays an essential role in the folding and function of important cellular proteins including steroid hormone receptors, protein kinases and proteins controlling the cell cycle and apoptosis. A 15 Å deep pocket region in the N-terminal domain of Hsp90 serves as an ATP/AD...

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Bibliographic Details

Published in:	Cell Stress Chaperones
Main Authors:	Schulte, Theodor W., Akinaga, Shiro, Soga, Shiro, Sullivan, William, Stensgard, Bridget, Toft, David, Neckers, Leonard M.
Format:	Artigo
Language:	Inglês
Published:	Elsevier 1998
Subjects:	Original Articles
Online Access:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC312953/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9672245/ https://ncbi.nlm.nih.govhttps://doi.org/10.1379/1466-1268(1998)003<0100:arbttn>2.3.co;2
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