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. Author manuscript; available in PMC: 2018 May 5.
Published in final edited form as: Biochem J. 2015 Jun 1;468(2):283–291. doi: 10.1042/BJ20141492

Figure 3. Effect of the SH2-N-lobe interaction on imatinib binding.

Figure 3

Imatinib binding rates (kon) of the SH2-KD construct and two mutants thereof referenced to that of the isolated kinase domain. Formation of the native SH2-N-lobe interface decreases the rate of drug binding and is reduced further by the mutation T231R. Mutational perturbation of the interface (I164E), however, enhances the binding rate compared to the wildtype.