OB-fold: Growing Bigger with Functional Consistency

Title: OB-fold: Growing Bigger with Functional Consistency

Volume: 4 Issue: 3

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

Affiliation:

Keywords: ob-fold, ob-folded proteins

Abstract: 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.

Cite this article as:

Agrawal Vishal and Kishan V. Radha K., OB-fold: Growing Bigger with Functional Consistency, Current Protein & Peptide Science 2003; 4 (3) . https://dx.doi.org/10.2174/1389203033487207