Molecular characterization of the gerbil C5a receptor and identification of a transmembrane domain V amino acid that is crucial for small molecule antagonist interaction.

@article{Waters2005MolecularCO,
  title={Molecular characterization of the gerbil C5a receptor and identification of a transmembrane domain V amino acid that is crucial for small molecule antagonist interaction.},
  author={Stephen M Waters and Robbin M Brodbeck and Jeremy Steflik and Jianying Yu and Carolyn O Baltazar and Amy E Peck and Daniel L. Severance and Lu Zhang and Kevin P M Currie and Bertrand Leo Chenard and Alan J. Hutchison and George D. Maynard and James E. Krause},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 49},
  pages={
          40617-23
        }
}
Anaphylatoxin C5a is a potent inflammatory mediator associated with pathogenesis and progression of several inflammation-associated disorders. Small molecule C5a receptor (C5aR) antagonist development is hampered by species-specific receptor biology and the associated inability to use standard rat and mouse in vivo models. Gerbil is one rodent species reportedly responsive to small molecule C5aR antagonists with human C5aR affinity. We report the identification of the gerbil C5aR cDNA using a… CONTINUE READING

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