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Published November 21, 1995 | Published
Journal Article Open

Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG

Abstract

The neonatal Fc receptor (FcRn) transports maternal IgG from ingested milk in the gut to the bloodstream of newborn mammals. An FcRn dimer was observed in crystals of the receptor alone and of an FcRn-Fc complex, but its biological relevance was unknown. Here we use surface plasmon resonance-based biosensor assays to assess the role of FcRn dimerization in IgG binding. We find high-affinity IgG binding when FcRn is immobilized on a biosensor chip in an orientation facilitating dimerization but not when its orientation disrupts dimerization. This result supports a model in which IgG-induced dimerization of FcRn is relevant for signaling the cell to initiate endocytosis of the IgG-FcRn complex.

Additional Information

© 1995 National Academy of Sciences. Communicated by Norman Davidson, California Institute of Technology, Pasadena, CA, July 28, 1995 (received for review June 1, 1995). We thank D. Vaughn, W. P. Burmeister, and J. Harber for critical review of the manuscript and A. Chirino for help in making Fig. 1. This work was supported by the Howard Hughes Medical Institute (P.J.B.), a postdoctoral fellowship from the Cancer Research Institute (M.R.), and a Caltech Summer Undergraduate Research Fellowship (Y.W.). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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