Extended Data Figure 8: NMR analysis of phosphorylated Ubl.
From: Mechanism of phospho-ubiquitin-induced PARKIN activation
a, BEST-TROSY spectra for isotope-labelled HsPARKIN Ubl domain (dark green) and phospho-Ubl domain (light green) with resonances assigned for the Ubl domain. b, Chemical shift perturbation of Ubl with respect to phospho-Ubl, showing significant perturbations in the region of phosphorylation (Ser65), the last β-strand and neighbouring β-strands. Grey bars, exchange broadened resonances. c, Mapping of perturbed resonances onto the previously determined NMR structure of HsPARKIN Ubl (PDB 1IYF (ref. 36)). The perturbed residues cluster in the Ser65-containing loop and in proximity to the Ile44 patch of the Ubl. d, Mapping of the perturbed resonances to the structure of RnPARKIN (PDB 4K95 (ref. 16)) shows that they perturb the interface between the Ubl domain and the PARKIN core. Thus, phosphorylated Ubl may not be able to (re)bind PARKIN at the same binding site.
