The contribution of the exosite residues of plasminogen activator inhibitor-1 to proteinase inhibition.

@article{Ibarra2004TheCO,
  title={The contribution of the exosite residues of plasminogen activator inhibitor-1 to proteinase inhibition.},
  author={Catherine A Ibarra and Grant Ellsworth Blouse and Thomas D Christian and Joseph D. Shore},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 5},
  pages={3643-50}
}
The binding of plasminogen activator inhibitor-1 (PAI-1) to serine proteinases, such as tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), is mediated by the exosite interactions between the surface-exposed variable region-1, or 37-loop, of the proteinase and the distal reactive center loop (RCL) of PAI-1. Although the contribution of such interactions to the inhibitory activity of PAI-1 has been established, the specific mechanistic steps affected by… CONTINUE READING

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