Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A POTENTIAL SH3 DOMAIN-BINDING SITE IN THE CRK SH2 DOMAIN
Autore:
ANAFI M; ROSEN MK; GISH GD; KAY LE; PAWSON T;
Indirizzi:
MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAM MOL BIOL & CANC,600 UNIV AVE TORONTO ON M5G 1X5 CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAM MOL BIOL & CANC TORONTO ON M5G 1X5 CANADA UNIV TORONTO,DEPT MOL & MED GENET TORONTO ON M5S 1A8 CANADA UNIV TORONTO,PROT ENGN NETWORK CTR EXCELLENCE TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT BIOCHEM TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT CHEM TORONTO ON M5S 1A8 CANADA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 35, volume: 271, anno: 1996,
pagine: 21365 - 21374
SICI:
0021-9258(1996)271:35<21365:APSDSI>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-ABL; C-13-LABELED PROTEINS; HIGH-AFFINITY; WW DOMAIN; SRC; PEPTIDE; IDENTIFICATION; PHOSPHATASE; SPECIFICITY; SUBSTRATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
M. Anafi et al., "A POTENTIAL SH3 DOMAIN-BINDING SITE IN THE CRK SH2 DOMAIN", The Journal of biological chemistry, 271(35), 1996, pp. 21365-21374

Abstract

The Src homology 2 (SH2) domain of the mammalian adaptor protein Crk-II contains a proline-rich insert, predicted to lie within an extendedDE loop, which is dispensable for phosphopeptide binding, Using the yeast two-hybrid system, this region of the Crk-II SH2 domain was foundto interact with a subset of SH3 domains, notably the Abl SH3 domain. Furthermore, this proline-rich insert was found to modify the efficiency with which Crk-II was phosphorylated by the p140(c-abl) tyrosine kinase, In vitro, the interaction of full length non-phosphorylated Crk-II with a glutathione S-transferase Abl SH3 domain fusion protein wasvery weak, However, phosphorylation of Crk-II on Tyr-221 which induces an intramolecular association with the SH2 domain, or addition of a phosphopeptide corresponding to the Crk-II Tyr-221 phosphorylation site, stimulated association of Crk-II with the Abl SH3 domain, NMR spectroscopic analysis showed that binding of the Tyr-221 phosphopeptide tothe Crk SH2 domain induced a chemical shift change in Val-71, locatedin the proline-rich insert, indicative of a change in the structure of the proline-rich loop in response of Crk SH2 pTyr-221 interaction, These results suggest that the proline-rich insert in the Crk SH2 domain constitutes an SH3 domain-binding site that can be regulated by binding of a phosphopeptide ligand to the Crk SH2 domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:28:20