Agrawal, Vishal and Kishan, K V Radha (2003) OB-fold: growing bigger with functional consistency. Current protein & peptide science, 4 (3). pp. 195-206. ISSN 1389-2037
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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.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Bentham Science. |
| Uncontrolled Keywords: | OB-fold: Growing Bigger with Functional Consistency |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 06 Jan 2012 14:58 |
| Last Modified: | 06 Jan 2012 14:58 |
| URI: | http://crdd.osdd.net/open/id/eprint/243 |
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