Kinase proteins have been intensively investigated as drug targets for decades because of their crucial involvement in many biological pathways. Most kinase drugs target the catalytic ATP pocket, which is highly conserved across the kinome, and as such often leads to potential side effects. It is thus highly desirable to develop non-ATP-competitive drugs that inhibit kinase activity via allosteric interactions. However, to elucidate the complex allosteric mechanism, it is essential to build a novel method to characterize a comprehensive non-catalytic pocket for the structurally well-covered hu...
