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

Proc Natl Acad Sci U S A. 1985 Aug;82(15):4954-8. doi: 10.1073/pnas.82.15.4954.

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.

MeSH terms

  • Animals
  • Binding Sites
  • Calcium / metabolism
  • Calcium-Binding Proteins* / metabolism
  • Calmodulin* / metabolism
  • Computers
  • Ions
  • Models, Molecular
  • Parvalbumins / metabolism
  • Peptides / metabolism
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Calcium-Binding Proteins
  • Calmodulin
  • Ions
  • Parvalbumins
  • Peptides
  • Calcium