Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: structural analysis of the binding site.

@article{Watt2001HomophilicAO,
  title={Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: structural analysis of the binding site.},
  author={Suzanne M. Watt and Ana Teixeira and G. Q. Zhou and Regis Doyonnas and Yawei Zhang and Fritz Grunert and Richard S Blumberg and Misao Kuroki and Keith M Skubitz and Paul A. Bates},
  journal={Blood},
  year={2001},
  volume={98 5},
  pages={
          1469-79
        }
}
CEACAM1 on leukocytic, endothelial, and epithelial cells functions in homophilic adhesion, tumor suppression, regulating cell adhesion and proliferation, and in heterophilic adhesion as a receptor for E-selectin and Neisseria meningiditis, Neisseria gonorrhoeae, Haemophilus influenzae, and murine coronaviruses. The 8 transmembrane isoforms of human CEACAM1 possess an extracellular N-terminal IgV domain, followed by variable numbers of IgC2 domains. To establish which key amino acids contribute… CONTINUE READING

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