Mapping the interaction of bradykinin 1-5 with the exodomain of human protease activated receptor 4.

@article{Nieman2005MappingTI,
  title={Mapping the interaction of bradykinin 1-5 with the exodomain of human protease activated receptor 4.},
  author={Marvin T. Nieman and Eileen Pag{\'a}n-Ramos and Mark Warnock and Yelena Krijanovski and Ahmed Khairul Hasan and Alvin H Schmaier},
  journal={FEBS letters},
  year={2005},
  volume={579 1},
  pages={
          25-9
        }
}
The angiotensin converting enzyme breakdown product of bradykinin, bradykinin 1-5 (RPPGF), inhibits thrombin-induced human or mouse platelet aggregation. RPPGF binds to the exodomain of human protease-activated receptor 1 (PAR1). Studies determined if RPPGF also binds to the exodomain of human PAR4. RPPGF binds to a peptide of the thrombin cleavage site on PAR4. Recombinant wild-type and mutated exodomain of human PAR4 was prepared. The N-terminal arginine on RPPGF binds to the P2 position or… CONTINUE READING

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Bradykinin and its metabolite bradykinin 1-5 inhibit thrombin-induced platelet aggregation in humans.

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