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 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Goto K,Toyama A,Takeuchi H,Takayama K,Saito T,Iwamoto M,Yeh JZ,Narahashi T

doi

10.1016/S0014-5793(04)00114-0

keywords:

subject

Has Abstract

pub_date

2004-03-12 00:00:00

pages

51-7

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579304001140

journal_volume

561

pub_type

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