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Fig. 2 | Molecular Neurodegeneration

Fig. 2

From: The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity

Fig. 2

Protein docking of the kinase PINK1 and the substrate Ub. a Structural model of a PINK1 p.I368N homodimer docked with Ub in the kinase domain (between the N- and C-lobe). One molecule of the PINK1 dimer is shown in electrostatic surface rendering. The other one is shown in ribbons colored according to the individual domains of PINK1. The p-Ser228, p-Ser402, and Asn368 residues are shown in licorice sticks with the carbons colored in gray. ATP is shown in licorice rendering with orange carbons. The substrate Ub is shown in yellow-green surface culled to reveal Ser65 residue in VdW. Both sides of the dimer are rotated 180°. b Zoom into the active site region. Left panel: PINK1 WT (residues Ile368, p-Ser228, and p-Ser402 are highlighted) docked with ATP (terminal phosphate is highlighted), and Ub (Ser-65 is highlighted). Right panel: PINK1 p.I368N mutant with the same residues highlighted for comparison. c Metric for enzymatic comparison of the of PINK1 WT and p.I368N mutant is given in the table. Atomic distances between the docked Ub (Ser65-oxygen), the terminal phosphate of ATP (P*), and PINK1 residues (p-Ser228-oxygen, p-Ser402-oxygen, I368-Calpha or N368-Calpha) were determined

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