A Predicted Structure of Calmodulin Suggests an Electrostatic Basis for Its Function

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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1985-08, Vol.82 (15), p.4954-4958
Main Authors: O'Neil, Karyn T., DeGrado, William F.
Format: Article
Language:English
Subjects:
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Binding Sites
Biochemistry
Biodegradation
Biological and medical sciences
Calcium
Calcium - metabolism
Calcium-Binding Proteins - metabolism
Calmodulin - metabolism
Computer graphics
Computers
Crystal structure
Electrical potential
Electrostatics
Fundamental and applied biological sciences. Psychology
Ions
Modeling
Models, Molecular
Parvalbumins - metabolism
Peptides - metabolism
Protein Conformation
Proteins
Structure-Activity Relationship
Surface areas
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Summary: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 α -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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.82.15.4954