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

Mankil Jung; Hanjo Kim; Youp Nam Ki; Tai No Kyoung

doi:10.1016/j.bmcl.2005.04.041

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

Mankil Jung, Hanjo Kim, Youp Nam Ki, Tai No Kyoung

Research output: Contribution to journal › Article › peer-review

57 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	2994-2997
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	15
Issue number	12
DOIs	https://doi.org/10.1016/j.bmcl.2005.04.041
Publication status	Published - 2005 Jun 15

Bibliographical note

Funding Information:
This work was supported by the Korea Research Foundation Grant (KRF-2003-015-C00380).

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

Access to Document

10.1016/j.bmcl.2005.04.041

Cite this

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title = "Three-dimensional structure of Plasmodium falciparum Ca2+- ATPase(PfATP6) and docking of artemisinin derivatives to PfATP6",

abstract = "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.",

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AU - Ki, Youp Nam

AU - Kyoung, Tai No

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