STRUCTURE-BASED DISCOVERY OF A NEW CLASS OF HSP90 INHIBITORS
[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. 
Publication Abstract from PubMed
Docking-based virtual screening identified 1-(2-phenol)-2-naphthol compounds as a new class of Hsp90 inhibitors of low to sub-micromolar potency. Here we report the binding affinities and cellular activities of several members of this class. A high resolution crystal structure of the most potent compound reveals its binding mode in the ATP binding site of Hsp90, providing a rationale for the observed activity of the series and suggesting strategies for developing compounds with improved properties.
Structure-based discovery of a new class of Hsp90 inhibitors.,Barril X, Brough P, Drysdale M, Hubbard RE, Massey A, Surgenor A, Wright L Bioorg Med Chem Lett. 2005 Dec 1;15(23):5187-91. Epub 2005 Oct 3. PMID:16202589
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.