The interaction of Fc alpha RI with IgA and its implications for ligand binding by immunoreceptors of the leukocyte receptor cluster.

@article{Wines2001TheIO,
  title={The interaction of Fc alpha RI with IgA and its implications for ligand binding by immunoreceptors of the leukocyte receptor cluster.},
  author={Bruce D Wines and Caroline Tan Sardjono and Halina Trist and C S Lay and P Mark Hogarth},
  journal={Journal of immunology},
  year={2001},
  volume={166 3},
  pages={1781-9}
}
This study defines the molecular basis of the FcalphaRI (CD89):IgA interaction, which is distinct from that of the other leukocyte Fc receptors and their Ig ligands. A comprehensive analysis using both cell-free (biosensor) and cell-based assays was used to define and characterize the IgA binding region of FcalphaRI. Biosensor analysis of mutant FcalphaRI proteins showed that residues Y35, Y81, and R82 were essential for IgA binding, and R52 also contributed. The role of the essential residues… CONTINUE READING