Fig. 1: Structural characterization of osimertinib co-binding with different allosteric inhibitors. | Nature Communications

Fig. 1: Structural characterization of osimertinib co-binding with different allosteric inhibitors.

From: Molecular basis for cooperative binding and synergy of ATP-site and allosteric EGFR inhibitors

Fig. 1

a Chemical structures of ATP-competitive and allosteric inhibitors. b Crystal structure of EGFR(T790M/V948R) in complex with osimertinib and EAI045 (PDB 7JXM). The C-helix is colored red, Asp-Phe-Gly (DFG) motif in orange, ATP-site inhibitor in magenta, and allosteric inhibitor in green. c EGFR(L858R/V948R) in complex with osimertinib and JBJ-063 (PDB 7K1H). The P-loop and side chain of F723 from EGFR(L858R/V948R) in complex with AMP-PNP and JBJ-063 is shown in dark gray for comparison (PDB 7K1I). d EGFR(T790M/V948R) in complex with osimertinib and DDC4002 (PDB 6XL4).

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