Structure of the ATP‐binding domain of Plasmodium falciparum Hsp90

Medientyp: E-Artikel
Titel: Structure of the ATP‐binding domain of Plasmodium falciparum Hsp90
Beteiligte: Corbett, Kevin D.; Berger, James M.
Erschienen: Wiley, 2010
Erschienen in: Proteins: Structure, Function, and Bioinformatics
Sprache: Englisch
DOI: 10.1002/prot.22799
ISSN: 0887-3585; 1097-0134
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Beschreibung: <jats:title>Abstract</jats:title><jats:p>Hsp90 is an important cellular chaperone and attractive target for therapeutics against both cancer and infectious organisms. The Hsp90 protein from the parasite <jats:italic>Plasmodium falciparum</jats:italic>, the causative agent of malaria, is critical for this organism's survival; the anti‐Hsp90 drug geldanamycin is toxic to <jats:italic>P. falciparum</jats:italic> growth. We have solved the structure of the N‐terminal ATP‐binding domain of <jats:italic>P. falciparum</jats:italic> Hsp90, which contains a principal drug‐binding pocket, in both apo and ADP‐bound states at 2.3 Å resolution. The structure shows that <jats:italic>P. falciparum</jats:italic> 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 <jats:italic>P. falciparum</jats:italic>, and provide a scaffold for future drug‐discovery efforts. Proteins 2010; © 2010 Wiley‐Liss, Inc.</jats:p>

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