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Titolo:
Mapping the integrin alpha(v)beta(3)-ligand interface by photoaffinity cross-linking
Autore:
Bitan, G; Scheibler, L; Greenberg, Z; Rosenblatt, M; Chorev, M;
Indirizzi:
Bethivsrael Deaconess Med Ctr, Dept Med, Charles A Dana & Thorndike Labs, D Beth Israel Deaconess Med Ctr Boston MA USA 02215 ana & Thorndike Labs, D Harvard Univ, Sch Med, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 vard Univ, Sch Med, Boston, MA 02215 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 11, volume: 38, anno: 1999,
pagine: 3414 - 3420
SICI:
0006-2960(19990316)38:11<3414:MTIAIB>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET GLYCOPROTEIN-IIIA; ASP-BINDING DOMAIN; LIGAND-BINDING; ALPHA-V-BETA-3 INTEGRINS; VITRONECTIN RECEPTOR; BETA-3 SUBUNIT; CATION-BINDING; SITE; SPECIFICITY; RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Chorev, M Bethivsrael Deaconess Med Ctr, Dept Med, Charles A Dana & Thorndike Labs, D Beth Israel Deaconess Med Ctr 330 Brookline Ave,HIM 944 Boston MA USA 02215
Citazione:
G. Bitan et al., "Mapping the integrin alpha(v)beta(3)-ligand interface by photoaffinity cross-linking", BIOCHEM, 38(11), 1999, pp. 3414-3420

Abstract

Integrins are cell surface adhesion molecules involved in mediating cell-extracellular matrix interactions. High-resolution structural data are not available for these heterodimeric receptors. Previous cross-linking studies of integrins aimed at elucidating the nature of the receptor-ligand interface have been limited to identification of relatively large binding domains. To create reagents for "photoaffinity scanning"' of the RGD-binding site of human integrin alpha(v)beta(3), new conformationally constrained ligands were designed. These photoreactive ligands are based, on cycle Ac-[Cys-Asn-Dmt-Arg-Gly-Asp-Cys]-OH, which displays an affinity of 50 nM for alpha(v)beta(3), This molecular scaffold was modified at the C-terminus by a benzophenone-containing amino acid residue, L-4-benzoylphenylalanine (Bpa). At the N-terminus, a molecular lag was introduced in the form of radioactive iodine or biotin. The newly designed tagged photoreactive RGD-containing ligandsdisplay an affinity of 0.5-0.7 mu M for alpha(v)beta(3), and cross-link efficiently and specifically to the receptor. A 100 kDa band corresponding tothe beta(3) subunit-ligand conjugate was detected as the major cross-linking product. Cross-linking was dependent upon the presence of Ca2+ and Mg2+ ions, and was competitively inhibited by a nonphotoreactive ligand. Enzymatic and chemical digestions of the radiolabeled photoconjugate enabled identification of a 20-amino acid fragment between positions 99 and 118 in the beta(3) chain of the integrin as the contact domain for ligand at a site adjacent to the C-terminal portion of the RGD triad.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 17:05:14