Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator.

@article{Yang1998EngineeringBM,
  title={Engineering bidentate macromolecular inhibitors for trypsin and urokinase-type plasminogen activator.},
  author={Sally Yang and Charles S. Craik},
  journal={Journal of molecular biology},
  year={1998},
  volume={279 4},
  pages={1001-11}
}
Ecotin, a dimeric serine protease inhibitor from Escherichia coli, is a novel platform for inhibitor design. An approach using the three-dimensional structure of the ecotin-trypsin complex to guide combinatiorial design efforts was taken to create potent bidentate ecotin inhibitors for trypsin and human urokinase-type plasminogen activator (uPA). The ecotin surface loop that was redesigned is composed of residues 67 to 70 (60 s loop), and binds to the target protease at a region 25 A from the… CONTINUE READING
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