Patterns of Sequence Variation in Families of Homologous Proteins

  • Tom Blundell
  • Jon Cooper
  • Dan Donnelly
  • Huub Driessen
  • Yvonne Edwards
  • Frank Eisenmenger
  • Carlos Frazao
  • Mark Johnson
  • Karsten Niefind
  • Matthew Newman
  • John Overington
  • Andrej Sali
  • Christine Slingsby
  • V. Nalini
  • Zhanyang Zhu
Chapter
Part of the Advances in Life Sciences book series (ALS)

Summary

X-ray structure analyses of proteins and computational approaches to the comparison of three-dimensional structures provide a basis for understanding the nature of restraints on the diversity of sequences in families of homologous proteins. Detailed examples are provided by structures defined by X-ray analysis at Birkbeck for two families of homologous proteins, the beta/gamma crystallins (five proteins) and aspartic proteinases (five enzymes). In addition all families of proteins, for which two or more well-refined high-resolution structures are available in the Brookhaven Databank, have been compared. Residue to residue substitution tables have been calculated for amino acids classified according to residue type, secondary structure, accessibility of the sidechain, and existence of hydrogen bonds from sidechain to other sidechains or peptide carbonyl or amide functions. Distinct patterns of substitution characterize most classes especially where amino acid residues are both solvent inaccessible and hydrogen-bonded through their sidechains.

Keywords

Aspartic Proteinase Rous Sarcoma Virus Amide Function Imperial Cancer Research Fund sUbstitution Table 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Basel AG 1991

Authors and Affiliations

  • Tom Blundell
    • 1
  • Jon Cooper
    • 1
  • Dan Donnelly
    • 1
  • Huub Driessen
    • 1
  • Yvonne Edwards
    • 1
  • Frank Eisenmenger
    • 1
  • Carlos Frazao
    • 1
  • Mark Johnson
    • 1
  • Karsten Niefind
    • 1
  • Matthew Newman
    • 1
  • John Overington
    • 1
  • Andrej Sali
    • 1
  • Christine Slingsby
    • 1
  • V. Nalini
    • 1
  • Zhanyang Zhu
    • 1
  1. 1.Imperial Cancer Research Fund Unit of Structural Molecular Biology and Laboratory of Molecular Biology, Department of CrystallographyBirkbeck College, London UniversityLondonUK

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