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. Author manuscript; available in PMC: 2015 Jun 14.
Published in final edited form as: Nat Commun. 2014 Mar 3;5:3397. doi: 10.1038/ncomms4397

Figure 4. Mechanism of ANS induced stabilization of intemediate I2.

Figure 4

(left) ANS binding to the allosteric site adjacent to C-helix in c-src kinase stabilizes the intermediate conformation by blocking the interactions between Lys295 and Glu310. The hydrogen bond formation between Lys295 and Glu310 is required for the locking of the C-helix in the active conformation. The sulfonate group in the ANS forms a hydrogen-bond with the Lys295 thereby locking it in its inactive conformation. (right) ANS binding also pushes the C-helix away from the ATP binding pocket. Superimposition of the crystal structures of the inactive (cyan) and active (green) states of ATP-bound c-src kinase with the ANS-bound src-kinase (orange) reveals the distinct conformation of the c-helix in presence of ANS.