Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 12, Issue 7, Pages 628-629Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb947
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Funding
- Wellcome Trust Funding Source: Medline
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Artemisinins are the most important class of antimalarial drugs. They specifically inhibit PfATP6, a SERCA-type ATPase of Plasmodium falciparum. Here we show that a single amino acid in transmembrane segment 3 of SERCAs can determine susceptibility to artemisinin. An L263E replacement of a malarial by a mammalian residue abolishes inhibition by artemisinins. Introducing residues found in other Plasmodium spp. also modulates artemisinin sensitivity, suggesting that artemisinins interact with the thapsigargin-binding cleft of susceptible SERCAs.
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