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. Author manuscript; available in PMC: 2015 Sep 5.
Published in final edited form as: Chembiochem. 2014 Aug 8;15(13):1920–1930. doi: 10.1002/cbic.201400025

Figure 3.

Figure 3

Binding to PfPK5. (A)Structure of CDK 1/2 docked onto the PfPK5 crystal structure (pdb 1V0O). The protein kinase (pink) and CDK 1/2 carbon (grey), hydrogen (grey), nitrogen (blue), sulfur (yellow) and oxygen (red) atoms are shown. Hydrogen bonds are predicted to form (black dotted lines) between the thioamide proton of CDK 1/2 and Gln 84, and between the primary amine proton on aminotriazole and Asp 85 (bond lengths < 2.5 Å). (B) Percent binding of commercially available kinase inhibitors to PfPK5 at 10 μM. Significant binding (> 50%) is only observed with the known CDK inhibitors, flavopiridol, SNS-032 and CDK 1/2, and the PIK inhibitor PIK-75. (C) Competitive binding plot of CDK 1/2 (red curve), flavopiridol (black curve) and SNS-032 (blue curve) to PfPK5 where decrease in relative signal correlates with compound binding. Data in C were fit to a nonlinear regression equation (curves shown) to obtain Kd values.