Structural models for a series of allosteric inhibitors of igf1r kinase

HIGHLIGHTS

• What: The authors report the structural model of each indole-butyl-amine derivative in complex with IGF1RK and provide detailed structural analyses to provide a rationale for the observed differences in the activities of these allosteric inhibitors. The authors report the unique binding conformation of the most potent derivative, C11, and unravel the chemical basis for the design of potent allosteric inhibitors of IGF1RK. The authors show that an electron-donating group with two aromatic rings is responsible for crucial interactions with the 5-cyano indole (R2) in the binding pocket. The authors show that the key . . .
  

   

  

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