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Titolo:
Amino acid residues in the PSI domain and cysteine-rich repeats of the integrin beta(2) subunit that restrain activation of the integrin alpha(x)beta(2)
Autore:
Zang, Q; Springer, TA;
Indirizzi:
Harvard Univ, Sch Med, Dept Pathol, Ctr Blood Res, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 hol, Ctr Blood Res, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 10, volume: 276, anno: 2001,
pagine: 6922 - 6929
SICI:
0021-9258(20010309)276:10<6922:AARITP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND-BINDING REGION; I-DOMAIN; MONOCLONAL-ANTIBODY; A-DOMAIN; PROPELLER DOMAIN; LEUKOCYTE DIFFERENTIATION; CONFORMATIONAL-CHANGES; REGULATED EXPRESSION; P150,95 CD11C/CD18; RECOGNITION SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Springer, TA Harvard Univ, Sch Med, Dept Pathol, Ctr Blood Res, 200 Longwood Ave, Boston, MA 02115 USA Harvard Univ 200 Longwood Ave Boston MA USA 02115 A 02115 USA
Citazione:
Q. Zang e T.A. Springer, "Amino acid residues in the PSI domain and cysteine-rich repeats of the integrin beta(2) subunit that restrain activation of the integrin alpha(x)beta(2)", J BIOL CHEM, 276(10), 2001, pp. 6922-6929

Abstract

The leukocyte integrin alpha (X)beta (2) (p150,95) recognizes the iC3b complement fragment and functions as the complement receptor type 4. alpha (X)beta (2) is more resistant to activation than other beta (2) integrins and is inactive in transfected cells. However, when human alpha (X) is paired with chicken or mouse beta (2), alpha (X)beta (2) is activated for binding to iC3b. Activating substitutions were mapped to individual residues or groups of residues in the N-terminal plexin/semaphorin/integrin (PSI) domain and C-terminal cysteine-rich repeats 2 and 3. These regions are linked,by a long range disulfide bond. Substitutions in the PSI domain synergized with substitutions in the cysteine-rich repeats. Substitutions T4P, T22A, Q5255, and V526L gave full activation. Activation of binding to iC3b: correlated with exposure of the CBR LFA-1/2 epitope in cysteine-rich repeat 3. The datasuggest that the activating substitutions are present in an interface thatrestrains the human alpha (X)/human beta (2) integrin in the inactive state. The opening of this interface is linked to structural rearrangements in other domains that activate ligand binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 22:53:56