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Figure 2.
Figure 2. Structure of the Active Kinase Domain of FAK
(A) The structure of the FAK kinase domain phosphorylated by Src
is shown in ribbon representation (green) with the activation
loop in blue. The side chains of phosphotyrosines 576 and 577
and AMP-PNP, which is bound to the active site, are shown in
stick representation. A Mg^2+ ion at the active site is shown as
a yellow sphere.
(B) Close-up view of the activation loop
with the side chains of pY576, pY577, R569, and R545 and the
main chains of A579 and S580 shown in stick representation. A
network of hydrogen bonds (orange dashed lines) involving the
phosphate group of pY577 stabilizes the conformation of the
activation loop.
(C) Superposition of active and inactive
FAK kinases. The autoinhibited structure is shown with the FERM
domain as a surface representation (light blue), and the linker
and kinase domains are shown in a ribbon representation colored
yellow and red, respectively. The structure of the active kinase
domain (green ribbon and blue activation loop) is superimposed
based on the kinase C-lobes. The side chain of pY576 and the
main chain carbonyl of A579 in the active kinase (both residues
are shown in space filling representations) clash with the FERM
domain in the autoinhibited structure.
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