Title: Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction
Abstract: Restricted accessMoreSectionsView PDF ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InRedditEmail Cite this article Overington John , Johnson Mark S. , Šali Andrej and Blundell Tom L. 1990Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure predictionProc. R. Soc. Lond. B.241132–145http://doi.org/10.1098/rspb.1990.0077SectionRestricted accessArticleTertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction John Overington Google Scholar Find this author on PubMed Search for more papers by this author , Mark S. Johnson Google Scholar Find this author on PubMed Search for more papers by this author , Andrej Šali Google Scholar Find this author on PubMed Search for more papers by this author and Tom L. Blundell Google Scholar Find this author on PubMed Search for more papers by this author John Overington Google Scholar Find this author on PubMed , Mark S. Johnson Google Scholar Find this author on PubMed , Andrej Šali Google Scholar Find this author on PubMed and Tom L. Blundell Google Scholar Find this author on PubMed Published:22 August 1990https://doi.org/10.1098/rspb.1990.0077AbstractThe pattern of residue substitution in divergently evolving families of globular proteins is highly variable. At each position in a fold there are constraints on the identities of amino acids from both the three-dimensional structure and the function of the protein. To characterize and quantify the structural constraints, we have made a comparative analysis of families of homologous globular proteins. Residues are classified according to amino acid type, secondary structure, accessibility of the sidechain, and existence of hydrogen bonds from sidechain to other sidechains or peptide carbonyl or amide functions. There are distinct patterns of substitution especially where residues are both solvent inaccessible and hydrogen bonded through their sidechains. The patterns of residue substitution can be used to construct templates or to identify 'key' residues if one or more structures are known. Conversely, analysis of conversation and substitution across a large family of aligned sequences in terms of substitution profiles can allow prediction of tertiary environment or indicate a functional role. Similar analyses can be used to test the validity of putative structures if several homologous sequences are available.FootnotesThis text was harvested from a scanned image of the original document using optical character recognition (OCR) software. As such, it may contain errors. 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Publication Year: 1990
Publication Date: 1990-08-22
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 215
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