Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen.

@article{Ke1997IdentificationOA,
  title={Identification of a hydrophobic exosite on tissue type plasminogen activator that modulates specificity for plasminogen.},
  author={S H Ke and K Tachias and Doriano Lamba and Wolfram Bode and Edwin L. Madison},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 3},
  pages={1811-6}
}
A wide variety of important biological processes, including both the formation and dissolution of blood clots, depend on specific cleavage of individual target proteins by serine proteases. For example, tissue type plasminogen activator (t-PA), a trypsin-like enzyme that catalyzes the rate-limiting step of the endogenous fibrinolytic cascade, has only one… CONTINUE READING