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A predicted structure of calmodulin suggests an electrostatic basis for its function.

K T O'Neil·W F DeGrado
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Abstract

By using interactive computer graphics, two models for calmodulin have been constructed based on the structures of two functionally and structurally related proteins, intestinal calcium-binding protein and carp parvalbumin. The two models have been compared and contrasted to the parent proteins with respect to proportion of solvent-exposed hydrophobic residues, solvent-accessible surface area, and side-chain packing. Electrostatic potential surfaces generated for the models suggest a probable binding site for basic amphiphilic alpha-helical peptides located between the last E and F helices in the second domain of calmodulin. Both electrostatic and hydrophobic complementarity can contribute to stabilization of a peptide-protein complex in this region.

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AnimalsBinding SitesCalciumCalcium-Binding ProteinsCalmodulinComputersIonsModels, MolecularParvalbuminsPeptidesProtein ConformationStructure-Activity RelationshipJournal Article

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K T O'Neil, W F DeGrado. 1985. A predicted structure of calmodulin suggests an electrostatic basis for its function.. https://doi.org/10.1073/pnas.82.15.4954

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