Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor
- 1 November 1994
- journal article
- Published by Springer Nature in Nature
- Vol. 372 (6504), 336-343
- https://doi.org/10.1038/372336a0
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.Keywords
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