OB-fold: growing bigger with functional consistency.

Vishal Agrawal; K V Radha Kishan

doi:10.2174/1389203033487207

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OB-fold: growing bigger with functional consistency.

Vishal Agrawal·K V Radha Kishan

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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 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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Animals Bacterial Toxins Databases, Factual Humans Models, Molecular Oligonucleotides Oligosaccharides Peptide Fragments Protein Binding Protein Folding Protein Structure, Secondary Protein Structure, Tertiary RNA Ribosomal Proteins Journal Article Review

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Vishal Agrawal, K V Radha Kishan. 2003. OB-fold: growing bigger with functional consistency.. https://doi.org/10.2174/1389203033487207

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