There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
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.