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Titolo:
CHARACTERIZATION OF THE PHOSPHOTYROSINE-BINDING DOMAIN OF THE DROSOPHILA SHE PROTEIN
Autore:
LI SC; LAI KMV; GISH GD; PARRIS WE; VANDERGEER P; FORMANKAY J; 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 HOSP SICK CHILDREN,RES INST,DIV BIOCHEM RES TORONTO ON M5G 1X8 CANADA
Titolo Testata:
The Journal of biological chemistry
fascicolo: 50, volume: 271, anno: 1996,
pagine: 31855 - 31862
SICI:
0021-9258(1996)271:50<31855:COTPDO>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR RECEPTORS; TYROSINE PHOSPHORYLATION; SIGNAL-TRANSDUCTION; NUCLEOTIDE EXCHANGE; ADAPTER PROTEIN; GRB2; RAS; INSULIN; TRANSFORMATION; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
S.C. Li et al., "CHARACTERIZATION OF THE PHOSPHOTYROSINE-BINDING DOMAIN OF THE DROSOPHILA SHE PROTEIN", The Journal of biological chemistry, 271(50), 1996, pp. 31855-31862

Abstract

The phosphotyrosine-binding (PTB) domain of Drosophila Shc (dShc) binds in vitro to phosphopeptides containing the sequence motif NPXpY, and physically associates with the activated Drosophila epidermal growthfactor receptor homologue (DER) in vivo. The structural elements, specificity and binding kinetics of the dShc PTB domain have now been characterized. The dShc PTB domain appeared similar to the insulin-like receptor substrate-1 PTB domain in secondary structure as suggested by Fourier transform infrared spectroscopy. Surface plasmon resonance measurements indicated that the dShc PTB domain bound with high affinity to phosphopeptides (Der) derived from the Tyr(1228) site of the DER receptor. The kinetics of the dShc PTB domain-Der phosphopeptide interaction differed from those of a typical SH2 domain-ligand interaction, in that the PTB domain displayed slower on/off rates. Competition binding assays using truncated versions of the Der peptides revealed that high affinity binding to the dShc PTB domain requires, in addition to the NPXpY motif, the presence of hydrophobic residues at both positions-5 and -7 relative to phosphotyrosine. The dShc PTB domain showed a similar binding specificity to the human Shc (hShc) PTB domain, but subtle differences were noted; such that the hShc PTB domain bound preferentially to a phosphopeptide from the mammalian nerve growth factor receptor, whereas the dShc PTB domain bound preferentially to phosphopeptides from the Drosophila DER receptor. The invertebrate dShc PTB domain therefore possesses a binding specificity for tyrosine-phosphorylated peptides that is optimally suited for recognition of the activated DER receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:03:07