Calmodulin (CaM) is a calcium-binding regulatory protein that influences many key processes in eukaryotic cells. One such process is modulating calcium release from the sarcoplasmic reticulum of cardiac muscle cells by regulating the calcium channel RyR. This in turns regulates the relaxation rate of ventricular cardiomyocytes. Mutations in CaM can lead to several chronic heart diseases such as ventricular arrhythmias. One such mutation is Q136P where a glutamine residue in one of CaM’s calcium binding sites is replaced with a proline residue. In this study the calcium dependent dynamics and thermo-stability of the Q136P mutant were characterized using solution state nuclear magnetic resonance (NMR) and circular dichroism.

Structural and functional characterization of arrythmogenic Q136P calmodulin mutant

253rd National Meeting (2017)

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