The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites.

@article{Gale2000TheAL,
  title={The autolysis loop of activated protein C interacts with factor Va and differentiates between the Arg506 and Arg306 cleavage sites.},
  author={Andrew J Gale and Mary Jo Heeb and John H. Griffin},
  journal={Blood},
  year={2000},
  volume={96 2},
  pages={585-93}
}
The anticoagulant human plasma serine protease, activated protein C (APC), inactivates blood coagulation factors Va (FVa) and VIIIa. The so-called autolysis loop of APC (residues 301-316, equivalent to chymotrypsin [CHT] residues 142-153) has been hypothesized to bind FVa. In this study, site-directed mutagenesis was used to probe the role of the charged residues in this loop in interactions between APC and FVa. Residues Arg306 (147 CHT), Glu307, Lys308, Glu309, Lys311, Arg312, and Arg314 were… CONTINUE READING
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Site-specific analysis of mutational 592 GALE et al BLOOD

  • E. Di Cera
  • Adv Protein
  • 2000

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