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Titolo:
Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand
Autore:
Sanchez, LM; Penny, DM; Bjorkman, PJ;
Indirizzi:
CALTECH, Dept Biol 15629, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 CH, Dept Biol 15629, Pasadena, CA 91125 USA CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 ard Hughes Med Inst, Pasadena, CA 91125 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 29, volume: 38, anno: 1999,
pagine: 9471 - 9476
SICI:
0006-2960(19990720)38:29<9471:SOTIBT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
I-RELATED RECEPTOR; CRYSTAL-STRUCTURE; MHC; BINDING; IGG; CRYSTALLIZATION; GLYCOSYLATION; EXPRESSION; FRAGMENTS; AFFINITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Bjorkman, PJ CALTECH, Dept Biol 15629, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 15629, Pasadena, CA 91125 USA
Citazione:
L.M. Sanchez et al., "Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand", BIOCHEM, 38(29), 1999, pp. 9471-9476

Abstract

The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, providing passive immunity and protecting serum IgG from degradation. For both functions, FcRn binds to IgG at the acidic pH of intracellular vesicles (pH less than or equal to 6.5) and releases IgG at the basic pH of the bloodstream (pH similar to 7.4). Crystallographic studies show that rat FcRn can interact with the Fc portion of IgG in a repeating array in which FcRn dimers are bridged by Fc fragments to create an "oligomeric ribbon" with a 2n:n stoichiometry. The stoichiometry of the interaction between soluble FcRn and Fc has been reported as either 2:1 for rat FcRn [Huber et al. (1993) J. Mol. Biol. 230, 1077-1083] or 1:1 for mouse FcRn [Popov et al. (1996) Mol. Immunol. 33, 521-530]. To ascertain the reasons for this difference, we analyzed complexes formed in solution between soluble rat or mouse FcRn and Fc. Using a gel-filtration assay under nonequilibrium conditions, we find that both forms of FcRn produce 2:1 receptor-ligand complexes, but that alterations of the carbohydrate moieties on mouse FcRn can result inan apparent stoichiometry of 1:1. However, under equilibrium conditions, all forms of FcRn make complexes with a 2:1 stoichiometry. We conclude that rat and mouse FcRn share the same general ligand binding properties but that small differences in affinities can produce apparent differences under nonequilibrium conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 10:05:36