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Figure 4.
Figure 4 Mode of PD 173074 binding to FGFR1K. (A) Stereo view of
the PD 173074 binding pocket in FGFR1K. The side chains of
residues that interact with the inhibitor are shown as well as
main-chain atoms that participate in hydrogen bonding.
Split-bond coloring is used with carbon atoms orange (PD 173074)
or green (FGFR1K), oxygen atoms red, nitrogen atoms blue and
sulfur atoms yellow. The FGFR1K main-chain representation is
colored light blue for the nucleotide-binding loop, purple for
the segment connecting the two kinase lobes, yellow for the
catalytic loop and orange for the activation loop. Hydrogen
bonds are shown as dashed lines. (B) Superposition of PD 173074
and AMP-PCP (Mohammadi et al., 1996a) bound to FGFR1K. View is
approximately perpendicular to the
pyrido[2,3-d]pyrimidine/adenine rings. Bonds and carbon atoms
are colored orange (PD 173074), green (FGFR1K) or gray
(AMP-PCP). Other atoms colored as in (A) with phosphorus atoms
black. Hydrogen bonds are shown as black (AMP-PCP) or orange (PD
173074) dashed lines. Due to disorder, the  phosphate
of AMP-PCP is not modeled. Prepared with GRASP (Nicholls et al.,
1991).
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