Modeling the mutational effects on calmodulin structure: prediction of alteration in the amino acid interactions.

Abstract excerpt

Calmodulin (CaM) is a highly conserved 17kDa eukaryotic protein that can bind specifically to over 100 protein targets in response to a Ca2+ signal. Present study was planned to mutate the crucial residues of N-terminal lobe, central helix, and C-terminal lobe that play important roles in activating and binding of enzymes. In all, 10 mutations were carried out in the predicted 3D structure of calmodulin using the...

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