Shah Figure 1.
Shah Figure 1. Schematic of binding modes of clinically active BCR-ABL kinase inhibitors. “Active” refers to the open conformation of BCR-ABL that is compatible with ATP binding and hydrolysis. “Inactive” refers to the closed conformation that is not catalytically active. The ability to bind to various BCR-ABL kinase domain conformations was determined by co-crystal studies, except when marked with an asterisk (*), which reflects results of computer modeling–based studies of binding. “Other targets” lists notable kinases that are reported to be inhibited at concentrations required to inhibit BCR-ABL activity.

Schematic of binding modes of clinically active BCR-ABL kinase inhibitors. “Active” refers to the open conformation of BCR-ABL that is compatible with ATP binding and hydrolysis. “Inactive” refers to the closed conformation that is not catalytically active. The ability to bind to various BCR-ABL kinase domain conformations was determined by co-crystal studies, except when marked with an asterisk (*), which reflects results of computer modeling–based studies of binding. “Other targets” lists notable kinases that are reported to be inhibited at concentrations required to inhibit BCR-ABL activity.

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