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

@article{Murzin1993OBoligonucleotideoligosaccharideBC,
  title={OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.},
  author={Alexey G. Murzin},
  journal={The EMBO journal},
  year={1993},
  volume={12 3},
  pages={
          861-7
        }
}
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
Highly Influential
This paper has highly influenced 21 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
Highly Cited
This paper has 452 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 273 extracted citations

Structure and dynamics study of translation initiation factor 1 from Staphylococcus aureus suggests its RNA binding mode.

Biochimica et biophysica acta. Proteins and proteomics • 2017
View 10 Excerpts
Highly Influenced

452 Citations

02040'94'99'05'11'17
Citations per Year
Semantic Scholar estimates that this publication has 452 citations based on the available data.

See our FAQ for additional information.