Three-dimensional structure of Plasmodium falciparum Ca2+-ATPase(PfATP6) and docking of artemisinin derivatives to PfATP6
Three-dimensional structure of Plasmodium falciparum Ca2+-ATPase(PfATP6) and docking of artemisinin derivatives to PfATP6
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DOI：
10.1016/j.bmcl.2005.04.041
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发表时间：
2005-06-15
影响因子：
2.7
通讯作者：
No, KT
中科院分区：
文献类型：
--
作者：
Jung, M;Kim, H;No, KT
通过同源模建和青蒿素衍生物与PfATP 6蛋白模型的对接模拟构建了PfATP 6的三维结构。对接和随后的LUDI评分显示与体外抗疟活性有良好的关系。青蒿素与PfATP 6的主要结合来源是疏水相互作用，生物学上重要的过氧键暴露在结合口袋的外部。这项研究表明，结合青蒿素的PfATP 6之前激活过氧化物键的Fe 2+物种。(c)2005爱思唯尔有限公司保留所有权利。
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 Fe2+ species. (c) 2005 Elsevier Ltd. All rights reserved.