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Copyright ©2013 Baishideng.
World J Virol. May 12, 2013; 2(2): 71-78
Published online May 12, 2013. doi: 10.5501/wjv.v2.i2.71
Figure 1
Figure 1 Diagram representing the domain organization of Src family kinases. As reported in the text, the C-terminus (C-t in the figure) when phosphorylated at Tyr527 binds to the Src homology (SH)2 domain and the polyproline type II helical motif (PPII) motif in the SH2 kinase linker (SH2-KL in the figure) engages the SH3 domain, thus inducing an inactive conformation. Disruption of these inhibitory interactions, in the case of viruses mostly induced by proteins bearing tyrosine phosphorylated or proline-rich motifs, leads to the full activation of Src family kinases.