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The regulation of the activity of Abl and Src family tyrosine kinases is
mediated by intramolecular interactions between the SH3, SH2, and kinase (SH1)
domains. We have determined the crystal structure of an unphosphorylated form of
c-Src in which the SH2 domain is not bound to the C-terminal tail. This results
in an open structure where the kinase domain adopts an active conformation and
the C terminus binds within a hydrophobic pocket in the C-terminal lobe.
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