OB-fold: growing bigger with functional consistency.
DIR@IMTECH: CSIR-Institute of Microbial Technology
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Title |
OB-fold: growing bigger with functional consistency.
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Creator |
Agrawal, Vishal
Kishan, K V Radha |
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Subject |
QR Microbiology
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Description |
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.
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Publisher |
Bentham Science
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Date |
2003-06
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Type |
Article
PeerReviewed |
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Relation |
http://www.benthamdirect.org/pages/dla-login.php
http://crdd.osdd.net/open/243/ |
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Identifier |
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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