Molecular mechanism of troponin-C function.

摘要: There is now a large body of evidence in support the view that Ca2+ binding to low affinity sites TnC induces movement helices B and C away from A D, thus opening hydrophobic cavity, site interaction with TnI. Another similar structure formed by helical segments C-terminal domain. Both appear interact inhibitory segment Whereas interactions at both are necessary for full regulatory activity TnC, domain stabilizes complex involving N-terminal directly linked release inhibition. In absence region TnI would preferentially bind actin on I II it switch TnC. Detachment gives rise further events thin filament regulation.