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Titolo:
THE STOICHIOMETRY AND AFFINITY OF THE INTERACTION OF MURINE FC FRAGMENTS WITH THE MHC CLASS I-RELATED RECEPTOR, FCRN
Autore:
POPOV S; HUBBARD JG; KIM JK; OBER B; GHETIE V; WARD ES;
Indirizzi:
UNIV TEXAS,SW MED CTR,DEPT MICROBIOL,5323 HARRY HINES BLVD DALLAS TX 75235 UNIV TEXAS,SW MED CTR,DEPT MICROBIOL DALLAS TX 75235 UNIV TEXAS,SW MED CTR,CTR CANC IMMUNOBIOL DALLAS TX 75235
Titolo Testata:
Molecular immunology
fascicolo: 6, volume: 33, anno: 1996,
pagine: 521 - 530
SICI:
0161-5890(1996)33:6<521:TSAAOT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE-PLASMON RESONANCE; IMMUNOGLOBULIN-G; IGG1 MOLECULE; MONOCLONAL-ANTIBODY; BINDING; COMPLEX; CRYSTALLIZATION; TRANSPORT; BIOSENSOR; REDUCTION;
Keywords:
FC RECEPTOR; RECOMBINANT FC FRAGMENT; AFFINITY; STOICHIOMETRY; TRANSCYTOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
S. Popov et al., "THE STOICHIOMETRY AND AFFINITY OF THE INTERACTION OF MURINE FC FRAGMENTS WITH THE MHC CLASS I-RELATED RECEPTOR, FCRN", Molecular immunology, 33(6), 1996, pp. 521-530

Abstract

The binding of recombinant wild type and mutant Fc-hinge fragments tosoluble, FcRn expressed in insect cells has been analysed. The mutantFc-hinge fragments are derived from murine IgG1 with mutation of residues located at the CH2-CH3 domain interface (Ile253, His310, Gln311, His433 and Asn434; EU numbering). These mutant Fc-hinge fragments havepreviously been shown to be deficient in neonatal transcytosis in suckling mice and also have abnormally short serum half lives. The mutated residues are highly conserved in human and rodent gammaglobulins (IgGs) and are also involved in binding to staphylococcal protein A. Thisstudy demonstrates that the Fc mutants have lower binding affinities for recombinant FcRn and mutations in the CH2 domain have a greater effect than those in the CH3 domain. There is an excellent correlation between affinity and transcytosis or the control of catabolism, and this provides further evidence in support of the close overlap of the sites of IgG/Fc involved in these processes. The stoichiometry of the FcRn:Fc interaction has also been investigated and has been found to be 1:1, indicating that binding of FcRn to one CH2-CH3 domain interface site precludes an FcRn:Fc interaction at the second site. Copyright (C) 1996 Elsevier Science Ltd.

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Documento generato il 27/11/20 alle ore 21:34:12