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 Lettjournal_title
FEBS lettersauthors
Goto K,Toyama A,Takeuchi H,Takayama K,Saito T,Iwamoto M,Yeh JZ,Narahashi Tdoi
10.1016/S0014-5793(04)00114-0keywords:
subject
Has Abstractpub_date
2004-03-12 00:00:00pages
51-7issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304001140journal_volume
561pub_type
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