OB-fold: Growing Bigger with Functional Consistency

Author(s): Vishal Agrawal , K. V. Radha Kishan .

Journal Name: Current Protein & Peptide Science

Volume 4 , Issue 3 , 2003

Become EABM
Become Reviewer


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 β-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.

Keywords: ob-fold, ob-folded proteins

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2003
Page: [195 - 206]
Pages: 12
DOI: 10.2174/1389203033487207
Price: $58

Article Metrics

PDF: 12