Figures
Rendering of Parkin's opening conformers resulting from molecular dynamics simulations.
Activation of Parkin by PINK1-dependent phosphorylation of Serine-65 initiates a cleft widening between the UBL domain and the adjacent linker region that propagates through release of the E2 binding region and further conformational adjustments of the active site region. The UBL domain begins its dynamic movement on the left side. Phospho-Ser65 is indicated by the 'black hole' in the UBL domain positioned on top right near the active site after its movement. See Caulfield et al.
Image Credit: Thomas R. Caulfield
Citation: (2014) PLoS Computational Biology Issue Image | Vol. 10(11) November 2014. PLoS Comput Biol 10(11): ev10.i11. https://doi.org/10.1371/image.pcbi.v10.i11
Published: November 20, 2014
Copyright: © 2014 Caulfield et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Activation of Parkin by PINK1-dependent phosphorylation of Serine-65 initiates a cleft widening between the UBL domain and the adjacent linker region that propagates through release of the E2 binding region and further conformational adjustments of the active site region. The UBL domain begins its dynamic movement on the left side. Phospho-Ser65 is indicated by the 'black hole' in the UBL domain positioned on top right near the active site after its movement. See Caulfield et al.
Image Credit: Thomas R. Caulfield