Title : NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos.

Pub. Date : 1994 Dec

PMID : 7773779






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Proline growth factor receptor bound protein 2 Homo sapiens
2 GRB2 couples receptor tyrosine kinase activation to Ras signalling by interacting, through its SH3 domains, to the carboxy-terminal proline-rich regions of the guanine nucleotide exchange factor Sos. Proline growth factor receptor bound protein 2 Homo sapiens
3 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos, shows that relative to the SH3 peptide complexes described for PI3K, Fyn and Abl, the proline-rich peptide in this complex binds in the opposite orientation. Proline growth factor receptor bound protein 2 Homo sapiens
4 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos, shows that relative to the SH3 peptide complexes described for PI3K, Fyn and Abl, the proline-rich peptide in this complex binds in the opposite orientation. Proline growth factor receptor bound protein 2 Homo sapiens