OB-fold domains: a snapshot of the evolution of sequence, structure and function

Curr Opin Struct Biol. 2002 Dec;12(6):794-801. doi: 10.1016/s0959-440x(02)00392-5.

Abstract

The OB-fold is found in all three kingdoms and is well represented in both sequence and structural databases. The OB-fold is a five-stranded closed beta barrel and the majority of OB-fold proteins use the same face for ligand binding or as an active site. Different OB-fold proteins use this 'fold-related binding face' to, variously, bind oligosaccharides, oligonucleotides, proteins, metal ions and catalytic substrates. Recently, a number of new structures with OB-folds have been reported that augment the variation seen for this set of proteins whilst conserving the characteristic fold and binding face. The conservation of fold and a functional binding face amongst many structures provides a model for investigating the evolutionary trajectory of sequence, structure and function.

Publication types

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

MeSH terms

  • Animals
  • Evolution, Molecular
  • Humans
  • Models, Molecular
  • Phylogeny
  • Protein Folding*
  • Protein Structure, Secondary*
  • Proteins / chemistry*
  • Proteins / classification
  • Proteins / metabolism

Substances

  • Proteins