title: Conservation of residue interactions in a family of Ca-binding proteins.
abstract: In the TNC family of Ca-binding proteins (calmodulin, parvalbumin, intestinal calcium binding protein and troponin C) approximately 70 well-conserved amino acid sequences and six crystal structures are known. We find a clear correlation between residue contacts in the structures and residue conservation in the sequences: residues with strong sidechain-sidechain contacts in the three-dimenesional structure tend to be the more conserved in the sequence. This is one way to quantify the intuitive notion of the importance of sidechain interactions for maintaining protein three-dimensional structure in evolution and may usefully be taken into account in planning point mutations in protein engineering.
authors: BIOcomputing Programme, EMBL, Heidelberg, FRG.
authors: A
authors: A
authors: Godzik
authors: C
authors: C
authors: Sander
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000235:genetics*; D003196:Computer Graphics; D001330:Electronic Data Processing; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D051381:Rats; D014961:X-Ray Diffraction
chemical_list: D002135:Calcium-Binding Proteins