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Crystal structure of the complex of rat neonatal Fc receptor with Fc

Nature volume 372, pages 379–383 (1994)Cite this article

Abstract

THE neonatal Fc receptor (FcRn) transports maternal immunoglobulin G (IgG) to the bloodstream of the newborn. FcRn is structurally similar to class I major histocompatibility complex (MHC) molecules1,2, despite differences in the ligands they bind (the Fc portion of IgG and antigenic peptides, respectively). A low-resolution crystal structure of the complex between FcRn and Fc localizes the binding site for Fc to the side of FcRn, distinct from the tops of the αl and α2 domains which serve as the peptide and T-cell receptor binding sites in class I molecules. FcRn binds to Fc at the interface between the Fc CH2 and CH3 domains, which contains several histidine residues that could account for the sharply pH-dependent FcRn/IgG interaction3. A dimer of FcRn heterodimers observed in the co-crystals and in the crystals of FcRn alone2 could be involved in binding Fc, correlating with the 2:1 binding stoichiometry between FcRn and IgG (ref. 4) and suggesting an unusual orientation of FcRn on the membrane.

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Author notes

  1. Andrew H. Huber

    Present address: Department of Cell Biology, Stanford University, Stanford, California, 94305, USA

Authors and Affiliations

  1. Division of Biology 156-29, California Institute of Technology, Pasadena, California, 91125, USA

    Wilhelm P. Burmeister

  2. Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California, 91125, USA

    Pamela J. Bjorkman

Authors
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  2. Andrew H. Huber
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  3. Pamela J. Bjorkman
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Burmeister, W., Huber, A. & Bjorkman, P. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372, 379–383 (1994). https://doi.org/10.1038/372379a0

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