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Figure 4.
(a) Correlation between IC[50] values for inhibitors against
Src (x axis) and either Hck or the gatekeeper mutant Src T338I
(y axis). (b) Binding orientation of S1 relative to ATP in c-Src
(top) and p110  (bottom).
(c) Overlay of cocrystal structures of inhibitors bound to c-Src
(protein colored red, drugs orange: S1, PP102, PP121 and PP494)
and p110 (protein
blue, compounds gray: S1 and S2). The gatekeeper residues Thr338
(c-Src) and Ile879 (p110 )
are highlighted. (d) Top, the catalytic lysine (Lys295) makes a
hydrogen bond to Glu310 in active c-Src. Center, helix C and
Glu310 are disordered in c-Src structures containing PP102.
Bottom, PP121 makes a hydrogen bond to Glu310 and orders helix C
when bound to c-Src.
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