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

Burmeister, W P; Gastinel, L N; Simister, N E; Blum, M L; Bjorkman, P J · Nature · 1994

basic_science · Level V

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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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