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Titolo:
Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II
Autore:
Li, YL; Li, HM; Dimasi, N; McCormick, JK; Martin, R; Schuck, P; Schlievert, PM; Mariuzza, RA;
Indirizzi:
Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA Univ Maryland Rockville MD USA 20850 Biotechnol, Rockville, MD 20850 USA Univ Minnesota, Sch Med, Dept Microbiol, Minneapolis, MN 55455 USA Univ Minnesota Minneapolis MN USA 55455 robiol, Minneapolis, MN 55455 USA NINDS, Neuroimmunol Branch, NIH, Bethesda, MD 20892 USA NINDS Bethesda MDUSA 20892 roimmunol Branch, NIH, Bethesda, MD 20892 USA NIH, Div Bioengn & Phys Sci, Bethesda, MD 20892 USA NIH Bethesda MD USA 20892 Div Bioengn & Phys Sci, Bethesda, MD 20892 USA
Titolo Testata:
IMMUNITY
fascicolo: 1, volume: 14, anno: 2001,
pagine: 93 - 103
SICI:
1074-7613(200101)14:1<93:CSOASB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
STAPHYLOCOCCAL-ENTEROTOXIN-A; COMPLEX CLASS-II; TOXIC SHOCK SYNDROME; BINDING-SITES; STREPTOCOCCUS-PYOGENES; MULTIPLE-SCLEROSIS; HLA-DR; PEPTIDE; APOPTOSIS; MOLECULE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Mariuzza, RA Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA Univ Maryland Rockville MD USA 20850 Rockville, MD 20850 USA
Citazione:
Y.L. Li et al., "Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II", IMMUNITY, 14(1), 2001, pp. 93-103

Abstract

MHC class II molecules possess two binding sites for bacterial superantigens (SAGs): a low-affinity site on the cu chain and a high-affinity, zinc-dependent site on the beta chain. only the former has been defined crystallographically. We report the structure of streptococcal pyrogenic exotoxin C (SPE-C) complexed with HLA-DR2a (DRA*010l, DRB5*0101) bearing a self-peptidefrom myelin basic protein (MBP). SPE-C binds the beta chain through a zincbridge that links the SAG and class II molecules. Surprisingly, SPE-C alsomakes extensive contacts with the MBP peptide, such that peptide accounts for one third of the surface area of the MHC molecule buried in the complex, similar to TCR-peptide/MHC complexes. Thus, SPE-C may optimize T cell responses by mimicking the peptide dependence of conventional antigen presentation and recognition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 06:20:11