Figure 7
Figure 7. Schematic of point mutations in the ABL kinase domain. Mutations in the ABL kinase domain (amino acids 240 to 500) cluster in 4 distinct regions, the ATP-binding domain (amino acid 248-255, green), mutations of T315 (red), which form a hydrogen bond with imatinib, M351 (turquoise), which interacts with the SH2 domain and participates in autoregulation of kinase activity, and the activation loop (amino acids 379-398, magenta). The vertical lines represent the frequency each amino acid has been found to be mutated as compiled from the literature. Reprinted from Deininger et al.41

Schematic of point mutations in the ABL kinase domain. Mutations in the ABL kinase domain (amino acids 240 to 500) cluster in 4 distinct regions, the ATP-binding domain (amino acid 248-255, green), mutations of T315 (red), which form a hydrogen bond with imatinib, M351 (turquoise), which interacts with the SH2 domain and participates in autoregulation of kinase activity, and the activation loop (amino acids 379-398, magenta). The vertical lines represent the frequency each amino acid has been found to be mutated as compiled from the literature. Reprinted from Deininger et al.41 

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