Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-3860
FEBS Lett 2004 Mar 12;5611-3:51-7. doi: 10.1016/S0014-5793(04)00114-0.
Show Gene links Show Anatomy links

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

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


???displayArticle.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.

???displayArticle.pubmedLink??? 15013750
???displayArticle.link??? FEBS Lett