The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif

The adapter Grb2 is an important mediator of normal cell proliferation and oncogenic signal transduction events. It consists of a central SH2 domain flanked by two SH3 domains. While the binding specificities of the Grb2 SH2 and N-terminal SH3 domain [Grb2 SH3(N)] have been studied in detail, bindin...

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Veröffentlicht in:	Oncogene 2001-03, Vol.20 (9), p.1052-1062
Hauptverfasser:	LEWITZKY, Marc, KARDINAL, Christian, GEHRING, Niels H, SCHMIDT, Enrico K, KONKOL, Birgit, EULITZ, Manfred, BIRCHMEIER, Walter, SCHAEPER, Ute, FELLER, Stephan M
Format:	Artikel
Sprache:	eng
Schlagworte:	Adapter proteins Adaptor Proteins, Signal Transducing Amino Acid Sequence Antigenic determinants Biological and medical sciences Blotting, Western c-Met protein Carrier Proteins - metabolism Cell physiology Cell proliferation Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cells, Cultured Consensus Sequence Conserved sequence Electrophoresis, Polyacrylamide Gel Epitopes Experiments Fundamental and applied biological sciences. Psychology Gab1 protein Glutathione Transferase - metabolism GRB2 Adaptor Protein Grb2 protein Homology Humans Kinases Molecular and cellular biology Molecular Sequence Data Mutants Oligodeoxyribonucleotides Oncology Peptide Fragments - metabolism Peptides Phosphoproteins - genetics Phosphoproteins - metabolism Point Mutation Precipitin Tests Proline - chemistry Protein Binding Protein-tyrosine kinase receptors Proteins Proteins - genetics Proteins - metabolism Rain and rainfall Recombinant Fusion Proteins - metabolism SH3 domain Signal transduction SLP-76 protein Spectrometry, Fluorescence src Homology Domains T cell receptors Tryptophan Tryptophan - chemistry Tyrosine
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