Conservation of residue interactions in a family of Ca-binding proteins |
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Authors: | Godzik Adam; Sander Chris |
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Affiliation: | 1BIOcomputing Programme, EMBL D-6900 Heidelberg, FRG
2Department of Biophysics, University of Warsaw Warsaw, Poland |
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Abstract: | In the TNC family of Ca-binding proteins (calmodulin, parvalbumin,intestinal calcium binding protein and troponin C) {small tilde}70 well-conserved amino acid sequences and six crystal structuresare known. We find a clear correlation between residue contactsin the structures and residue conservation in the sequences:residues with strong sidechainsidechain contacts in thethree-dimensional structure tend to be the more conserved inthe sequence. This is one way to quantify the intuitive notionof the importance of sidechain interactions for maintainingprotein three-dimensional structure in evolution and may usefullybe taken into account in planning point mutations in proteinengineering. |
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Keywords: | evolution/ protein structure/ mutability/ conservation/ contact maps |
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