Three-dimensional structure of Plasmodium falciparum Ca2+ -ATPase(PfATP6) and docking of artemisinin derivatives to PfATP6.

Construction of the 3D structure of PfATP6 by homology modeling and docking simulation of artemisinin derivatives to this protein model are reported. Docking and consequent LUDI scores show good relation with in vitro antimalarial activities. The main binding source of artemisinins to the PfATP6 is hydrophobic interaction and biologically important peroxide bonds were exposed to outside of the binding pocket. This study suggests binding of artemisinin to PfATP6 precedes activation of peroxide bond by Fe(2+) species.