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Titolo:
EVIDENCE THAT THE INTEGRIN BETA-3 AND BETA-5 SUBUNITS CONTAIN A METALION-DEPENDENT ADHESION SITE-LIKE MOTIF BUT LACK AN I-DOMAIN
Autore:
LIN ECK; RATNIKOV BI; TSAI PR; GONZALEZ ER; MCDONALD S; PELLETIER AJ; SMITH JW;
Indirizzi:
LA JOLLA CANC RES CTR,BURNHAM INST,PROGRAM CELL ADHES & EXTRACELLULARMATRIX LA JOLLA CA 92037 LA JOLLA CANC RES CTR,BURNHAM INST,PROGRAM CELL ADHES & EXTRACELLULARMATRIX LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT CELL BIOL LA JOLLA CA 92037
Titolo Testata:
The Journal of biological chemistry
fascicolo: 22, volume: 272, anno: 1997,
pagine: 14236 - 14243
SICI:
0021-9258(1997)272:22<14236:ETTIBA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND-BINDING; ALPHA(V) INTEGRINS; CRYSTAL-STRUCTURE; CATION-BINDING; CELL-ADHESION; A-DOMAIN; DIVALENT; PERSPECTIVES; ATTACHMENT; CD11B/CD18;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
E.C.K. Lin et al., "EVIDENCE THAT THE INTEGRIN BETA-3 AND BETA-5 SUBUNITS CONTAIN A METALION-DEPENDENT ADHESION SITE-LIKE MOTIF BUT LACK AN I-DOMAIN", The Journal of biological chemistry, 272(22), 1997, pp. 14236-14243

Abstract

The amino-terminal domain of each integrin beta subunit is hypothesized to contain an ion binding site that is key to cell adhesion, A new hypothesis regarding the structure of this site is suggested by the crystallization of the I domains of the integrin alpha(L) and alpha(M) subunits (Lee, J.-O., Rieu, P., Arnaout, M. A., and Liddington, R. (1995) Cell 80, 631-638; Qu, A., and Leahy, D. J. (1995) Proc. Natl, Acad,Sci, U.S.A. 92, 10277-10281), In those proteins, an essential metal ion is bound by a metal ion-dependent adhesion site (MIDAS), The MIDAS is presented at the apex of a larger protein module called an I domain, The metal ligands in the MIDAS can be separated into three distantlyspaced clusters of oxygenated residues, These three coordination sites also appear to exist in the integrin beta 3 and beta 5 subunits, Here, we examined the putative metal binding site within beta 3 and beta 5 using site-directed mutagenesis and ligand binding studies, We also investigated the fold of the domain containing the putative metal binding site using the PHD structural algorithm. The results of the study point to the similarity between the integrin beta subunits and the MIDAS motif at two of three key coordination points, Importantly though, the study failed to identify a residue in either beta subunit that corresponds to the second metal coordination group in the MIDAS, Moreover, structural algorithms indicate that the fold of the beta subunits isconsiderably different than the I domains, Thus, the integrin beta subunits appear to present a MIDAS-like motif in the context of a protein module that is structurally distinct from known I domains.

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Documento generato il 11/07/20 alle ore 07:49:42