The structural basis of sequence-independent peptide binding by OppA protein.

@article{Tame1994TheSB,
  title={The structural basis of sequence-independent peptide binding by OppA protein.},
  author={Jeremy R.H. Tame and Garib N Murshudov and Eleanor J. Dodson and Teresa K. Neil and Guy G. Dodson and Christopher F. Higgins and Anthony James Wilkinson},
  journal={Science},
  year={1994},
  volume={264 5165},
  pages={1578-81}
}
Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode… CONTINUE READING
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