Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
BS Knudsen, SM Feller, H Hanafusa - Journal of Biological Chemistry, 1994 - ASBMB
The widely expressed cellular Crk protein has the domain structure SH2-SH3-SH3. We have
previously demonstrated that the more N-terminal SH3 domain of Crk (CrkSH3 (N))
specifically binds several cytoplasmic proteins. A cDNA encoding one of these proteins was
isolated and found to have two different splice forms. The sequence is virtually identical to
C3G, a guanine-nucleotide exchange factor. The center region of the 145-155-kDa protein
contains four similar proline-rich sequences which are capable of binding individually to the …
previously demonstrated that the more N-terminal SH3 domain of Crk (CrkSH3 (N))
specifically binds several cytoplasmic proteins. A cDNA encoding one of these proteins was
isolated and found to have two different splice forms. The sequence is virtually identical to
C3G, a guanine-nucleotide exchange factor. The center region of the 145-155-kDa protein
contains four similar proline-rich sequences which are capable of binding individually to the …