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. Author manuscript; available in PMC: 2012 Jul 6.
Published in final edited form as: Nature. 2012 Apr 15;485(7397):260–263. doi: 10.1038/nature11016

Figure 2. Modelling of FLT3–AC220 interactions.

Figure 2

a, Docking model of the AC220-bound FLT3 kinase domain: AC220 (blue); activation loop (orange) and DFG motif (green); amino acid residues that confer AC220 resistance when mutated (F691, D835 and Y842) and that interact with AC220 (F691, C694 and F830) in sticks. b, Surface and stick presentation of AC220 and AC220-interacting residues on FLT3: the carbonyl oxygen of C694 interacts with one of the AC220 amide groups; F691 forms a π–π stacking interaction with AC220; F830 interacts with AC220 through a perpendicular aromatic–aromatic interaction. c, Structure of the activation loop: residues D835,Y842 and interacting residues on FLT3 depicted in sticks.