Binding site for IgE of the human lymphocyte low-affinity Fc epsilon receptor (Fc epsilon RII/CD23) is confined to the domain homologous with animal lectins.

@article{Bettler1989BindingSF,
  title={Binding site for IgE of the human lymphocyte low-affinity Fc epsilon receptor (Fc epsilon RII/CD23) is confined to the domain homologous with animal lectins.},
  author={B. Bettler and R. Maier and D. Rüegg and H. Hofstetter},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1989},
  volume={86 18},
  pages={
          7118-22
        }
}
  • B. Bettler, R. Maier, +1 author H. Hofstetter
  • Published 1989
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
The lymphocyte low-affinity receptor for IgE (Fc epsilon RII) is involved in two seemingly unrelated processes: (i) promotion of general B-cell growth and (ii) isotype-specific IgE synthesis. To characterize domains of Fc epsilon RII important for effector function, we have expressed Fc epsilon RII mutants in mammalian cells. The results show that the IgE-binding region of Fc epsilon RII corresponds almost exactly to a domain of 123 amino acid residues homologous with the carbohydrate-binding… Expand
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