title: OB-fold domains: a snapshot of the evolution of sequence, structure and function.
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.
authors.affiliation: AgResearch Laboratory for Structural Biology, School of Biological Sciences, University of Auckland, Private Bag 92-019, New Zealand. v.arcus@auckland.ac.nz
authors.forename: Vickery
authors.initials: V
authors.lastname: Arcus
mesh_terms: D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008958:Models, Molecular; D010802:Phylogeny; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism
chemical_list: D011506:Proteins