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Titolo:
HIGHLY CONSERVED AMINO-ACIDS IN THE SH2 AND CATALYTIC DOMAINS OF V-SRC ARE ALTERED IN NATURALLY-OCCURRING, TRANSFORMATION-DEFECTIVE ALLELES
Autore:
VERDERAME MF; VARMUS HE;
Indirizzi:
PENN STATE UNIV,COLL MED,DEPT MICROBIOL & IMMUNOL HERSHEY PA 17033 UNIV CALIF SAN FRANCISCO,DEPT MICROBIOL & IMMUNOL SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143
Titolo Testata:
Oncogene
fascicolo: 1, volume: 9, anno: 1994,
pagine: 175 - 182
SICI:
0950-9232(1994)9:1<175:HCAITS>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
TERMINAL REGULATORY DOMAIN; TYROSINE PROTEIN-KINASES; C-ABL; ONCOGENIC ACTIVATION; CELL-TRANSFORMATION; CRYSTAL-STRUCTURE; PHOSPHOLIPASE-C; POINT MUTATIONS; SARCOMA-VIRUS; PP60C-SRC;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
M.F. Verderame e H.E. Varmus, "HIGHLY CONSERVED AMINO-ACIDS IN THE SH2 AND CATALYTIC DOMAINS OF V-SRC ARE ALTERED IN NATURALLY-OCCURRING, TRANSFORMATION-DEFECTIVE ALLELES", Oncogene, 9(1), 1994, pp. 175-182

Abstract

We have identified 11 novel point mutations that abolish the transforming capacity of the oncogene v-src. These transformation-defective alleles were originally identified in morphologically flat subclones of rat cells transformed by wild type v-src. Nine of the mutations affectamino acid residues that are highly conserved in the catalytic domainof pp60(v-src) and completely abolish kinase activity. The other 2 mutations alter conserved residues in the SH2 domain (Phe-172 replaced with Val in one case [F172V] and Leu-186 replaced with Phe in the other[L186F]), drastically reducing, but not eliminating, kinase activity. The enzymatic and transforming functions of one of the SH2 mutants, L186F are host dependent; the mutant protein is active in chicken cells, but inactive in rat cells, as previously observed for some other SH2mutants. These results are interpreted in relation to the recently described three-dimensional structures of SH2 domains and of the catalytic domain of a protein kinase. In addition, they support a role for the SH2 domain in the regulation of kinase activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 10:26:55