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. Author manuscript; available in PMC: 2024 Dec 30.
Published in final edited form as: Mol Cell. 2023 May 18;83(10):1677–1692.e8. doi: 10.1016/j.molcel.2023.04.019

Figure 4. The human PER2 pFASP binds to the active site of CK1.

Figure 4.

a, Surface representation of CK1 catalytic domain bound to ADP (PDB 5X17). Spheres, sulfate anions from the crystallization condition bound at anion binding sites as indicated. b, Surface representation of the CK1 catalytic domain bound to a human PER2 3pFASP peptide (see Supplementary Figure 3a). c-e, Zoom of 3pFASP interactions within anion binding site 1 (c), the active site (d), and anion binding site 2 (e). f, Structural alignment showing the main chain for the activation loop of CK1 WT (gray) and the tau mutant (red) showing a clash of the 3pFASP (teal) with the conformation of the activation loop stabilized by the tau mutation. g, Characterization of key interactions from molecular dynamics simulations that stabilize the 5pFASP product in the active site, Site 1, Site 2, and an additional anion binding site located proximal to Site 2 (Site 3’). Histograms were computed based on distances sampled during the GaMD simulations.