Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor

Nature. 1994 Nov 24;372(6504):336-43. doi: 10.1038/372336a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Animals, Newborn / immunology*
  • Biological Evolution
  • Computer Graphics
  • Crystallography, X-Ray
  • Histocompatibility Antigens Class I / chemistry*
  • Immunoglobulin Fc Fragments / metabolism
  • Protein Binding
  • Protein Conformation
  • Rats
  • Receptors, Fc / chemistry*
  • Receptors, Fc / metabolism


  • Histocompatibility Antigens Class I
  • Immunoglobulin Fc Fragments
  • Receptors, Fc