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Ca 2+ binding sites in calmodulin and troponin C alter interhelical angle movements
Author(s) -
Goto Kunihiko,
Toyama Akira,
Takeuchi Hideo,
Takayama Kazuyoshi,
Saito Tsutomu,
Iwamoto Masatoshi,
Yeh Jay Z,
Narahashi Toshio
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00114-0
Subject(s) - calmodulin , troponin c , conformational change , chemistry , steric effects , biophysics , binding site , crystallography , molecular dynamics , stereochemistry , side chain , calcium binding protein , ef hand , calcium , troponin , biochemistry , computational chemistry , biology , enzyme , psychology , organic chemistry , psychiatry , myocardial infarction , polymer
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 Ca 2+ ions. Analyses of conformational changes in calmodulin and troponin C indicated that the shortening of the distance between Ca 2+ ions and Ca 2+ binding sites of helices caused widening of the distance between Ca 2+ 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.