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Figure 29 A schematic showing the regulation of Src tyrosine kinase between active and inactive states. (a) The inactive conformation is stabilised by intramolecular interactions between the SH2 domain and phosphorylated Tyr 527 in the C-terminal tail and between the SH3 domain and a specific sequence in the link between the SH2 domain and the kinase domain. (b) In the switch to the active conformation, these interactions are disrupted and the SH2 and SH3 domains dissociate and bind to other specific ligands. The inhibitory phosphate group on Tyr 527 is removed and Tyr 416 is phosphorylated. As a result, the activation loop adopts an open conformation and the peptide substrate can bind to the C lobe of the kinase domain. (Adapted from Huse and Kuriyan, 2002.)

 3.4 The functional domains of Src

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