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2000
Volume 4, Issue 3
  • ISSN: 1389-2037
  • E-ISSN: 1875-5550

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.

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/content/journals/cpps/10.2174/1389203033487207
2003-06-01
2025-08-11
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  • Article Type:
    Review Article
Keyword(s): ob-fold; ob-folded proteins
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