Elaborate manifold of short hydrogen bond arrays mediating binding of active site-directed serine protease inhibitors.

@article{Katz2003ElaborateMO,
  title={Elaborate manifold of short hydrogen bond arrays mediating binding of active site-directed serine protease inhibitors.},
  author={Bradley A. Katz and Kyle C Elrod and Erik Verner and Richard L Mackman and Christine Luong and William D Shrader and Martin Sendzik and Jeffrey R Spencer and Paul A. Sprengeler and Aleks Kolesnikov and Vincent W-F Tai and Hon C. Hui and James Guy Breitenbucher and Darin Allen and James W. Janc},
  journal={Journal of molecular biology},
  year={2003},
  volume={329 1},
  pages={93-120}
}
An extensive structural manifold of short hydrogen bond-mediated, active site-directed, serine protease inhibition motifs is revealed in a set of over 300 crystal structures involving a large suite of small molecule inhibitors (2-(2-phenol)-indoles and 2-(2-phenol)-benzimidazoles) determined over a wide range of pH (3.5-11.4). The active site hydrogen-bonding mode was found to vary markedly with pH, with the steric and electronic properties of the inhibitor, and with the type of protease… CONTINUE READING

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