Evolutionary predictions of binding surfaces and interactions

Curr Opin Struct Biol. 2002 Feb;12(1):21-7. doi: 10.1016/s0959-440x(02)00284-1.

Abstract

Rapid progress in structural biology and whole-genome sequencing technology means that, for many protein families, structural and evolutionary information are readily available. Recent developments demonstrate how this information can be integrated to identify canonical determinants of protein structure and function. Among these determinants, those residues that are on protein surfaces are especially likely to form binding sites and are the logical choice for further mutational analysis and drug targeting.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Binding Sites / physiology*
  • Catalytic Domain / physiology
  • Evolution, Molecular*
  • Forecasting
  • Humans
  • Ligands
  • Multigene Family
  • Protein Binding*
  • Protein Folding
  • Protein Interaction Mapping
  • Sequence Alignment

Substances

  • Ligands