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Fig. 1 | Molecular Cancer

Fig. 1

From: Discovery of a novel third-generation EGFR inhibitor and identification of a potential combination strategy to overcome resistance

Fig. 1

Chemical structure, binding mode and target inhibition of compound ASK120067. a Chemical structure of ASK120067. b Structure modeling of ASK120067 binding to EGFR T790M. The 2-aminopyrimidine core of ASK120067 forms two hydrogen bonds to the hinge residue Met793, and the acrylamide group forms a covalent bond with the conserved C797 residue in the ATP-binding pocket. The C5-Cl substitution points to the gatekeeper Met790 residue. The 2,4-disubstituted pyrimidine scaffold adapts a U-shaped configuration. The amine moiety faces an open space in the solvent exposure area. c Inhibition of ASK120067 on EGFR kinases determined by ELISA assay. IC50 values are shown as the mean ± SD from at least three independent experiments. d Kinase profiling of ASK120067 at a concentration of 100 nM against 258 human kinases. The graphic was generated by BioMed X GmbH and Merck KgaA, with slight modifications. Circles indicate detected kinases, and the circle size indicates the strength of inhibition

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Molecular Cancer

ISSN: 1476-4598