Computational studies of the binding mechanism of calmodulin with chrysin

被引:54
作者
Li, Lin
Wei, Dong-Qing [1 ]
Wang, Jing-Fang
Chou, Kuo-Chen
机构
[1] Shanghai Jiao Tong Univ, Coll Life Sci & Biotechnol, Shanghai 200240, Peoples R China
[2] Peking Univ, Dept Biochem & Mol Biol, Beijing 100871, Peoples R China
[3] Chinese Acad Sci, Bioinformat Ctr, Key Lab Syst Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China
[4] Gordon Life Sci Inst, San Diego, CA 92130 USA
基金
中国国家自然科学基金;
关键词
calmodulin; phosphorylated flavonoid; chrysin; binding pocket; molecular docking; molecular dynamics; escaping trajectory;
D O I
10.1016/j.bbrc.2007.05.053
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Calmodulin (CaM) plays a crucial role in metabolism and physiology of eukaryotes by regulating biological activities. Multiple lines of evidences indicate that the phosphorylated flavonoids possess relatively stronger affinities for proteins by forming non-covalent complexes with them, and that the cellular functions are often triggered by this kind of interactions. Chrysin is one of the phosphorylated flavonoids that exist ubiquitously in plants and have remarkably beneficial pharmacological effects. In this study, the molecular docking tools were utilized to investigate the interactions of CaM with chrysin. Two different favorable binding modes have been observed. To complement the results obtained by the molecular docking study, an in-depth investigation into the binding modes was conducted with the molecular dynamics (MD) simulation to explore the binding profile and energy landscape. Based on the results thus obtained, a clear definition of the binding pocket for each of the two binding modes has been revealed. These findings may shed light upon the binding interactions of CaM with chrysin, providing a solid molecular basis for subset analysis of its pharmacological benefits. (C) 2007 Elsevier Inc. All rights reserved.
引用
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页码:1102 / 1107
页数:6
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