High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds.

@article{Luckett1999HighresolutionSO,
  title={High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds.},
  author={S. Luckett and R. S. Biotechnology Garcia and John J. Barker and Alexander Konarev and Peter R. Shewry and Anthony R. Clarke and R. Leo Brady},
  journal={Journal of molecular biology},
  year={1999},
  volume={290 2},
  pages={
          525-33
        }
}
Proteinaceous serine proteinase inhibitors are widespread throughout the plant kingdom where they play an important role in protection against pests and pathogens. Here, we describe the isolation and characterisation of a novel 14 amino acid residue cyclic peptide from sunflower seeds, which is a potent inhibitor of trypsin (Ki=100 pM). The crystal structure of this peptide in complex with bovine beta-trypsin shows both sequence and conformational similarity with the trypsin-reactive loop of… 

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