HSP90 N-terminal domain in complex with (1R)-2-(5-chloro-2,4-dihydroxybenzoyl)-N-ethylisoindoline-1-carboxamide
[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
The discovery and optimization of potency and metabolic stability of a novel class of dihyroxyphenylisoindoline amides as Hsp90 inhibitors are presented. Optimization of a screening hit using structure-based design and modification of log D and chemical structural features led to the identification of a class of orally bioavailable non-quinone-containing Hsp90 inhibitors. This class is exemplified by 14 and 15, which possess improved cell potency and pharmacokinetic profiles compared with the original screening hit.
Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (hsp90) molecular chaperone.,Kung PP, Huang B, Zhang G, Zhou JZ, Wang J, Digits JA, Skaptason J, Yamazaki S, Neul D, Zientek M, Elleraas J, Mehta P, Yin MJ, Hickey MJ, Gajiwala KS, Rodgers C, Davies JF, Gehring MR J Med Chem. 2010 Jan 14;53(1):499-503. PMID:19908836
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.