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Titolo:
Complex structure of the activating immunoreceptor NKG2D and its MHC classI-like ligand MICA
Autore:
Li, PW; Morris, DL; Willcox, BE; Steinle, A; Spies, T; Strong, RK;
Indirizzi:
Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr Seattle WA USA 98109 , Seattle, WA 98109 USA CALTECH, Div Biol, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125CALTECH, Div Biol, Pasadena, CA 91125 USA Fred Hutchinson Canc Res Ctr, Div Clin Res, Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr Seattle WA USA 98109 , Seattle, WA 98109 USA
Titolo Testata:
NATURE IMMUNOLOGY
fascicolo: 5, volume: 2, anno: 2001,
pagine: 443 - 451
SICI:
1529-2908(200105)2:5<443:CSOTAI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
NATURAL-KILLER-CELLS; DELTA T-CELLS; CRYSTAL-STRUCTURE; INHIBITORY RECEPTOR; HLA-E; RECOGNITION; BINDING; MOLECULES; EXPRESSION; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Strong, RK Fred Hutchinson Canc Res Ctr, Div Basic Sci, 1124 Columbia St, Seattle, WA98109 USA Fred Hutchinson Canc Res Ctr 1124 Columbia St Seattle WA USA 98109
Citazione:
P.W. Li et al., "Complex structure of the activating immunoreceptor NKG2D and its MHC classI-like ligand MICA", NAT IMMUNOL, 2(5), 2001, pp. 443-451

Abstract

The major histocompatibility complex (MHC) class I homolog, MICA, is a stress-inducible ligand for NKG2D, a C-type lectin-like activating immunoreceptor,The crystal structure of this ligand-receptor complex that we report here reveals an NKG2D homodimer bound to a MICA monomer in an interaction that is analogous to that seen in T cell receptor-MHC class I protein complexes. Similar surfaces on each NKG2D monomer interact with different surfaces on either the alpha1 or alpha2 domains of MICA.The binding interactions arelarge in area and highly complementary.The central section of the alpha2-domain helix, disordered in the structure of MICA alone, is ordered in the complex and forms part of the NKG2D interface.The extensive flexibility of the interdomain linker of MICA is shown by its altered conformation when crystallized alone or in complex with NKG2D.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:25:43