Ca2+ binding sites in calmodulin and troponin C alter interhelical angle movements

FEBS Letters

Saito, Tsutomu⁴  Narahashi, Toshio²  Goto, Kunihiko²  Takayama, Kazuyoshi⁴  Toyama, Akira³  Yeh, Jay Z²  Iwamoto, Masatoshi¹  Takeuchi, Hideo³ 

[1] Department of Applied Physics, Tohoku Gakuin University, 1-13-1, Tagajyo, Miyagi 985-8537, Japan;Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, IL 60611-3008, USA;Department of Pharmaceuticals, Graduate School of Pharmaceutical Sciences, Tohoku University, Aobayama, Sendai 980-8578, Japan;Shock Wave Research Center, Institute of Fluid Science, Tohoku University, 2-1-1, Katahira, Sendai 980-8577, Japan

关键词: Molecular dynamics;    Conformational change;    Calcium binding protein;    EF hand;    Root mean square difference;    Alpha-helix;    CaM;    calmodulin;    TnC;    troponin C;    RMSD;    root mean square difference;   

DOI  :  10.1016/S0014-5793(04)00114-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Molecular dynamics analyses were performed to examine conformational changes in the C-domain of calmodulin and the N-domain of troponin C induced by binding of Ca²⁺ ions. Analyses of conformational changes in calmodulin and troponin C indicated that the shortening of the distance between Ca²⁺ ions and Ca²⁺ binding sites of helices caused widening of the distance between Ca²⁺ binding sites of helices on opposite sides, while the hydrophobic side chains in the center of helices hardly moved due to their steric hindrance. This conformational change acts as the clothespin mechanism.

【 授权许可】

Unknown