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XB-ART-1789
Nat Struct Mol Biol 2005 Jul 01;127:628-9. doi: 10.1038/nsmb947.
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A single amino acid residue can determine the sensitivity of SERCAs to artemisinins.

Uhlemann AC , Cameron A , Eckstein-Ludwig U , Fischbarg J , Iserovich P , Zuniga FA , East M , Lee A , Brady L , Haynes RK , Krishna S .


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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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