Structural basis of pH-dependent antibody binding by the neonatal Fc receptor.

@article{Vaughn1998StructuralBO,
  title={Structural basis of pH-dependent antibody binding by the neonatal Fc receptor.},
  author={Daniel E. Vaughn and Pamela J. Bjorkman},
  journal={Structure},
  year={1998},
  volume={6 1},
  pages={63-73}
}
BACKGROUND The neonatal Fc receptor (FcRn) mediates the transcytosis of maternal immunoglobulin G (IgG) across fetal and/or neonatal tissues for the acquisition of passive immunity. In adults, FcRn is involved in the maintenance of high serum IgG levels. Both processes are mediated by pH-dependent IgG binding to FcRn-FcRn binds to IgG with nanomolar affinity at pH 6, but shows no detectable binding at pH 7.5. At pH 6, FcRn is more thermally stable and the dissociation rate of its light chain is… CONTINUE READING

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