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

Kunihiko Goto; Akira Toyama; Hideo Takeuchi; Kazuyoshi Takayama; Tsutomu Saito; Masatoshi Iwamoto; Jay Z. Yeh; Toshio Narahashi

doi:10.1016/S0014-5793(04)00114-0

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

Kunihiko Goto^*, Akira Toyama, Hideo Takeuchi, Kazuyoshi Takayama, Tsutomu Saito, Masatoshi Iwamoto, Jay Z. Yeh, Toshio Narahashi

^*Corresponding author for this work

Pharmacology

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

12 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	51-57
Number of pages	7
Journal	FEBS Letters
Volume	561
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(04)00114-0
State	Published - Mar 12 2004

Keywords

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

ASJC Scopus subject areas

Genetics
Molecular Biology
Biophysics
Structural Biology
Biochemistry
Cell Biology

Access to Document

10.1016/S0014-5793(04)00114-0

Cite this

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title = "Ca2+ binding sites in calmodulin and troponin C alter interhelical angle movements",

abstract = "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.",

keywords = "Alpha-helix, CaM, calmodulin, Calcium binding protein, Conformational change, EF hand, Molecular dynamics, RMSD, root mean square difference, Root mean square difference, TnC, troponin C",

author = "Kunihiko Goto and Akira Toyama and Hideo Takeuchi and Kazuyoshi Takayama and Tsutomu Saito and Masatoshi Iwamoto and Yeh, {Jay Z.} and Toshio Narahashi",

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T1 - Ca2+ binding sites in calmodulin and troponin C alter interhelical angle movements

AU - Goto, Kunihiko

AU - Toyama, Akira

AU - Takeuchi, Hideo

AU - Takayama, Kazuyoshi

AU - Saito, Tsutomu

AU - Iwamoto, Masatoshi

AU - Yeh, Jay Z.

AU - Narahashi, Toshio

PY - 2004/3/12

Y1 - 2004/3/12

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AB - 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.

KW - Alpha-helix

KW - CaM, calmodulin

KW - Calcium binding protein

KW - Conformational change

KW - EF hand

KW - Molecular dynamics

KW - RMSD, root mean square difference

KW - Root mean square difference

KW - TnC, troponin C

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