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

Research output: Contribution to journalArticlepeer-review

11 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 languageEnglish (US)
Pages (from-to)51-57
Number of pages7
JournalFEBS Letters
Volume561
Issue number1-3
DOIs
StatePublished - 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

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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