Molecular dynamics simulations revealed Ca2+-dependent conformational change of Calmodulin

被引：59

作者：

Komeiji, Y

Ueno, Y

Uebayasi, M

机构：

[1] Natl Inst Adv Ind Sci & Technol, AIST, RICS, IMCB, Tsukuba, Ibaraki 3058566, Japan

[2] Natl Inst Adv Ind Sci & Technol, AIST, CBRC, NRI, Tsukuba, Ibaraki 3058566, Japan

来源：

FEBS LETTERS | 2002年 / 521卷 / 1-3期

关键词：

calmodulin; molecular dynamics; computer simulation; calcium; conformation; PEACH; GRAPE;

D O I：

10.1016/S0014-5793(02)02853-3

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：

Molecular dynamics simulations were performed to simulate Ca2+-dependent conformational change of calmodulin (CaM). Simulations of the fully Ca2+-bound form of CaM (Holo-CaM) and the Ca2+-free form (Apo-CaM) were performed in solution for 4 ns starting from the X-ray crystal structure of Holo-CaM. A striking difference was observed between the trajectories of Holo-CaM and Apo-CaM: the central helix remained straight in the former but became largely bent in the latter. Also, the flexibility of Apo-CaM was higher than that of Holo-CaM. The results indicated that the bound Ca2+ ions harden the structure of CaM. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：133 / 139

页数：7

共 43 条

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