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. Author manuscript; available in PMC: 2020 Aug 1.
Published in final edited form as: Cancer Discov. 2019 May 20;9(8):1064–1079. doi: 10.1158/2159-8290.CD-19-0182

Figure 4. Structural modeling of secondary FGFR2 kinase domain mutations with TAS-120.

Figure 4.

A, Model showing TAS-120 docked into ATP-binding pocket of wild type FGFR2. Amino acid residues corresponding to mutations conferring resistance to ATP competitive FGFR inhibitors are highlighted. Structural representations were prepared using PyMOL.

B, A close-up view of TAS-120 in ATP-binding pocket of wild type FGFR2. The gatekeeper residue (V565) is in close proximity to dimethoxy phenyl group of TAS-120.