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Curr Opin Struct Biol. 2002 Dec;12(6):794-801.

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

Author information

1
AgResearch Laboratory for Structural Biology, School of Biological Sciences, University of Auckland, Private Bag 92-019, New Zealand. v.arcus@auckland.ac.nz

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.

PMID:
12504685
[Indexed for MEDLINE]

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