Binding structure of elastase inhibitor scyptolin A.

@article{Matern2003BindingSO,
  title={Binding structure of elastase inhibitor scyptolin A.},
  author={U. Matern and C. Schleberger and S. Jelakovic and J. Weckesser and G. Schulz},
  journal={Chemistry & biology},
  year={2003},
  volume={10 10},
  pages={
          997-1001
        }
}
  • U. Matern, C. Schleberger, +2 authors G. Schulz
  • Published 2003
  • Chemistry, Medicine
  • Chemistry & biology
  • Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.8 A resolution. The inhibitor occupies the most prominent subsites S1 through S4 of… CONTINUE READING
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