Structure of the ATP-binding domain of Plasmodium falciparum Hsp90

Kevin D. Corbett, James M. Berger

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


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 Å 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.

Original languageEnglish (US)
Pages (from-to)2738-2744
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Issue number13
StatePublished - Oct 2010
Externally publishedYes


  • ATPase
  • Drug design
  • GHKL fold
  • Malaria

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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