Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
MULTIPLE LOOP STRUCTURES CRITICAL FOR LIGAND-BINDING OF THE INTEGRIN ALPHA-4 SUBUNIT IN THE UPPER FACE OF THE BETA-PROPELLER MODE-1
Autore:
IRIE A; KAMATA T; TAKADA Y;
Indirizzi:
SCRIPPS CLIN & RES INST,DEPT VASC BIOL,10555 N TORREY PINES RD LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT VASC BIOL LA JOLLA CA 92037
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 14, volume: 94, anno: 1997,
pagine: 7198 - 7203
SICI:
0027-8424(1997)94:14<7198:MLSCFL>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION; MELANOMA ADHESION; VLA-4; FIBRONECTIN; RECEPTOR; SITE; IDENTIFICATION; ATTACHMENT; DISTINCT; VCAM-1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
A. Irie et al., "MULTIPLE LOOP STRUCTURES CRITICAL FOR LIGAND-BINDING OF THE INTEGRIN ALPHA-4 SUBUNIT IN THE UPPER FACE OF THE BETA-PROPELLER MODE-1", Proceedings of the National Academy of Sciences of the United Statesof America, 94(14), 1997, pp. 7198-7203

Abstract

A non-I-domain integrin, alpha 4 beta 1, recognizes vascular cell adhesion molecule 1 (VCAM-1) and the IIICS portion of fibronectin. To localize regions of alpha 4 critical for ligand binding, we swapped several predicted loops within or near the putative ligand-binding site of alpha 4 (which spans repeats 25 of the seven N-terminal repeats) with the corresponding regions of alpha 5. Swapping residues 112-131 in repeat 2, or residues 237-247 in repeat 4, completely blocked adhesion toimmobilized VCAM-1 and connecting segment 1 (CS-1) peptide. However, swapping residues 4062 in repeat 1, residues 151-164 in repeat 3, or residues 282-288 (which contain a putative cation binding motif) in repeat 5 did not affect or only slightly reduced adhesion to these ligands. The binding of several function-blocking antibodies is blocked by swapping residues 112-131, 151-164, and 186-191 (which contain previously identified residues critical for ligand binding, Tyr-187 and Gly-190). These results are consistent with the recently published beta-propeller folding model of the integrin alpha 4 subunit [Springer, T. A. (1997) Proc. Natl. Acad. Sci. USA 94, 65-72], in which seven four-stranded beta-sheets are arranged in a torus around a pseudosymmetric axis. The regions of alpha 4 critical for ligand binding are adjacent to each other and are located in the upper face, the predicted ligand-binding site, of the beta-propeller model, although they are not adjacent in the primary structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:10:11