Abstract
The three-dimensional structure of the rat neonatal Fc receptor (FcRn) is similar to the structure of molecules of the major histocompatibility complex (MHC). The counterpart of the MHC peptide-binding site is closed in FcRn, making the FcRn groove incapable of binding peptides. A dimer of FcRn heterodimers seen in the crystals may represent a receptor dimer that forms when the Fc portion of a single immunoglobulin binds. An alternative use of the MHC fold for immune recognition is indicated by the FcRn and FcRn/Fc co-crystal structures.
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Burmeister, W., Gastinel, L., Simister, N. et al. Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature 372, 336–343 (1994). https://doi.org/10.1038/372336a0
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DOI: https://doi.org/10.1038/372336a0
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