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Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor

West, Anthony P., Jr. and Bjorkman, Pamela J. (2000) Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor. Biochemistry, 39 (32). pp. 9698-9708. ISSN 0006-2960. http://resolver.caltech.edu/CaltechAUTHORS:20170131-083605849

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Abstract

The neonatal Fc receptor (FcRn) performs two distinct but related functions:  transport of maternal immunoglobulin G (IgG) to pre- or neonatal mammals, thus providing passive immunity, and protection of IgG from normal serum protein catabolism. FcRn is related to class I MHC proteins but lacks a functional peptide binding groove. The crystal structure of human FcRn has been determined at 2.7 Å resolution and compared to the previously described structure of rat FcRn [Burmeister et al. (1994) Nature 372, 336−343] and to the structures of MHC and MHC-related proteins. Human FcRn is structurally similar to the rat receptor but does not form receptor dimers in the crystals as observed in crystals of rat FcRn. The interaction between human FcRn and IgG was characterized by determining the binding stoichiometry using equilibrium gel filtration and by deriving binding affinities for the different human IgG subclasses using a surface plasmon resonance assay. Like rat and mouse FcRn, human FcRn interacts with IgG with a 2:1 receptor:ligand stoichiometry. The binding of human FcRn to the four human IgG subclasses shows subclass and allotype variations but no clear subclass affinity differences that correlate with serum half-lives. The structure of human FcRn and studies of its ligand binding are relevant to current efforts to use FcRn-mediated regulation of IgG half-life in serum to increase the lifetimes of antibody-based therapeutics.


Item Type:Article
Related URLs:
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http://dx.doi.org/10.1021/bi000749mDOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi000749mPublisherArticle
ORCID:
AuthorORCID
Bjorkman, Pamela J.0000-0002-2277-3990
Additional Information:© 2000 American Chemical Society. Received 3 April 2000. Published online 18 July 2000. Published in print 1 August 2000. We thank N. E. Simister for the cDNA encoding hFcRn, W. Lance Martin, Clinton White, Tara Chapman, Art Chirino, and Dan Vaughn for helpful discussions, G. Hathaway and the Caltech PPMAL for protein sequencing analysis, and members of the Bjorkman laboratory for critical reading of the manuscript.
Record Number:CaltechAUTHORS:20170131-083605849
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20170131-083605849
Official Citation:Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor Anthony P. West, Jr. and Pamela J. Bjorkman Biochemistry 2000 39 (32), 9698-9708 DOI: 10.1021/bi000749m
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:73850
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:31 Jan 2017 17:36
Last Modified:31 Jan 2017 17:36

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