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Figure 7.
Cartoon Representation of Fes Activation In its unligated and
unphosphorylated state, the Fes SH2 domain (blue), [alpha]C
(red), and activation segment (purple) are significantly
disordered (left). Binding of a primed peptide (yellow)
stabilizes the SH2 domain, leading to a productive orientation
of the SH2 domain, with respect to the kinase domain, and stable
positioning of [alpha]C (middle). Phosphorylation of the
activation segment at Y713 and binding of the substrate molecule
to the kinase domain stabilizes the activation segment in a
conformation suitable for catalysis (right). Cell. 2008
September 5; 134(5): 793–803. doi: 10.1016/j.cell.2008.07.047.
Copyright [copyright] 2008 ELL & Excerpta Medica
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