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Figure 5.
FIGURE 5. Portions of the FERM kinase linker including the
Src SH3 binding site and the Tyr397 autophosphorylation site are
tethered across the surface of the F1 and F3 subdomains in the
FAK405 structure. A, ribbon and transparent surface
representation of the FAK FERM domain. The Src SH3 binding site
is shown in green (residues 363-375) and the Tyr397-containing
segment (residues 394-403) is colored in pink. B, detail of the
interactions between the Src SH3-binding site and the surface of
F3. Hydrogen bonds between the RXXPXXP motif (residues Arg368 to
Pro374) and the F3 lobe are indicated by dashed lines and
involve the side chains of Gln303 and Gln317 on the F3 lobe. C,
details of the interaction between the FAK autophosphorylation
Tyr397 segment and the F1 lobe. Hydrogen bonds are indicated
with dashed lines and involve the side chains of Glu403 with
His41 and Ser54 bonds. Tyr397 is surface exposed and not
phosphorylated in the structure.
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