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![[Figure 9]](gm5080fig9mag.jpg)
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Figure 9
(a) Interactions between the SH2–kinase linker (grey) and the SH3 domain (green). Residues of the SH2 and kinase domains that also interact with the SH3 domain in the structure of the c-Src kinase (PDB entry 2ptk) are shown as orange sticks. The interactions between residues in the SH3 domain and SH2–kinase linker (shown as sticks) are marked by green dashed lines. The three interaction pockets are marked in orange and labelled P1, P2 and P3. (b) Superposition of the SH3 domain of the c-Src kinase and the v-Src SH3 Q128R mutant (PDB entry 7ner, yellow, cartoon). The oncogenic mutations Trp95 and Asn117 are shown as yellow sticks and the interactions established by Arg95 and Asp117 have been removed. (c) Closed inactive conformation of the c-Src tyrosine kinase from chicken (PDB entry 2ptk). The SH1-domain N- and C-terminal lobes are coloured magenta and pink, respectively. The SH2 domain is coloured blue and the SH2–SH1 linker cyan. The SH3 domain is shown in green and the superposition of v-Src SH3 is shown in yellow. The mutated residues in the SH3 domain are shown as sticks. |
![[Figure 9]](gm5080fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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