3k60

Publication Abstract from PubMed

Hsp90 is an important cellular chaperone and attractive target for therapeutics against both cancer and infectious organisms. The Hsp90 protein from the parasite Plasmodium falciparum, the causative agent of malaria, is critical for this organism's survival; the anti-Hsp90 drug geldanamycin is toxic to P. falciparum growth. We have solved the structure of the N-terminal ATP-binding domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, in both apo and ADP-bound states at 2.3 A resolution. The structure shows that P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents such as geldanamycin in an identical manner. Our results should aid in the structural understanding of Hsp90-drug interactions in P. falciparum, and provide a scaffold for future drug-discovery efforts. Proteins 2010; (c) 2010 Wiley-Liss, Inc.

Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.,Corbett KD, Berger JM Proteins. 2010 Jun 14. PMID:20635416^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.