Surface map comparison: Studying function diversity of homologous proteins

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27 Scopus citations

Abstract

A simplified protein surface cartography approach has been developed to assist in the analysis of surface features in homologous families, and thus to predict conservation or divergence of protein functions and protein-protein interaction patterns. A spherical approximation of protein surface was used, with a focus on charged and hydrophobic residues. The resulting surface map allows for qualitative analysis and comparison of surfaces of proteins, but can also be used to define a simple numerical measure of map similarity between two or more proteins. The latter was shown to be useful for function based classifications within large protein families. Surface map analysis was tested on several test cases: haemoglobins, death domains and TRAF domains. It was shown that surface map comparison allows a better function prediction than general sequence analysis methods and can reproduce known examples of functional variation within a divergent group of proteins. In another example, we predict novel, unexpected sets of common functional properties for seemingly distant members of a large group of divergent proteins. The method was also shown to be robust enough to allow using protein models from comparative modelling instead of experimental structures.

Original languageEnglish (US)
Pages (from-to)793-806
Number of pages14
JournalJournal of Molecular Biology
Volume309
Issue number3
DOIs
StatePublished - Jun 8 2001
Externally publishedYes

Keywords

  • Protein cartography
  • Protein function prediction
  • Protein structure prediction
  • Protein surface maps
  • Sequence analysis

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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