Title : Identification and functional characterization of an Src homology domain 3 domain-binding site on Cbl.

Pub. Date : 2006 Dec

PMID : 17094785






7 Functional Relationships(s)
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1 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
2 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
3 We previously showed that the primary interaction between Src and Cbl is mediated by the Src homology domain 3 (SH3) of Src binding to proline-rich sequences of Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
4 Mutating prolines 543-548 reduced Src binding to the Cbl 479-636 fragment significantly more than mutating the prolines in the PPVPPR(494-499) motif, which was previously reported to bind Src SH3. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
5 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
6 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens
7 Mutating Cbl prolines 543-548 to alanines substantially reduced Src binding to Cbl, Src-induced phosphorylation of Cbl, and the inhibition of Src kinase activity by Cbl. Proline SRC proto-oncogene, non-receptor tyrosine kinase Homo sapiens