A single amino acid residue can determine the sensitivity of SERCAs to artemisinins.

Nat. Struct. Mol. Biol.2005 Jul;12(7):628-9. Epub 2005 Jun 05

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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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A single amino acid residue can determine the sensitivity of SERCAs to artemisinins.

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