%0 Journal Article
%@ 1389-2037
%A Agrawal, Vishal
%A Kishan, K V Radha
%D 2003
%F open:243
%I Bentham Science
%J Current protein & peptide science
%K OB-fold: Growing Bigger with Functional Consistency 
%N 3
%P 195-206
%T OB-fold: growing bigger with functional consistency.
%U http://crdd.osdd.net/open/243/
%V 4
%X It was predicted that the folding space for various protein sequences is restricted and a maximum of 1000 protein folds could be expected. Although, there were about 648 folds identified, general functional features of individual folds is not thoroughly studied. We selected OB-fold, which is supposed to be an oligonucleotide and oligosaccharide binding fold to study the general functional features. OB-fold is a small beta-barrel fold formed from 5 strands connected by modulating loops. We observed consistently 2 or 3 loops on the same face of barrel acting as clamps to bind to their ligands. Depending on the ligand, which could be a single or double stranded DNA/RNA or an oligosaccharide, and their conformational properties the loops change in length and sequence to accommodate various ligands. Different classes of OB-folded proteins were analyzed and found that the functional features are retained in spite of negligible sequence homology among various proteins studied.
%Z Copyright of this article belongs to Bentham Science.