Fig. 4: Conformational changes resulting from binding of ATPγS–(Mg2+)2 and competitive inhibitors. | Nature

Fig. 4: Conformational changes resulting from binding of ATPγS–(Mg2+)2 and competitive inhibitors.

From: Structural insights into inhibitor regulation of the DNA repair protein DNA-PKcs

Fig. 4

a, The p-loop conformation in apo DNA-PKcs (pink) is fixed by the flanking β-sheets and the electrostatic interaction between Arg3733 and Asp3587. b, Two views, related by rotation of 120o, of the effect of binding different ligands on the conformation of the p-loop. These conformational changes resemble the movement of a spring leaf. The corresponding movement of the flanking β-sheets transmits a conformational change to the core DNA-PKcs kinase region. Grey, ATPγS; green, wortmannin; blue, NU7441; purple, AZD7648; cyan, M3814. c, Orthogonal views of the p-loop conformations regulating the conformation of the DNA-PKcs kinase region, including the PRD.

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