OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.

  title={OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.},
  author={Alexey G. Murzin},
  journal={The EMBO journal},
  volume={12 3},
A novel folding motif has been observed in four different proteins which bind oligonucleotides or oligosaccharides: staphylococcal nuclease, anticodon binding domain of asp-tRNA synthetase and B-subunits of heat-labile enterotoxin and verotoxin-1. The common fold of the four proteins, which we call the OB-fold, has a five-stranded beta-sheet coiled to form a closed beta-barrel. This barrel is capped by an alpha-helix located between the third and fourth strands. The barrel-helix frameworks can… CONTINUE READING
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