Figure 3.

Parkin His302 and Lys151 are required for optimal binding with ubiquitin^{Phospho-Ser65}

1. Parkin H302A and K151A mutants exhibit marked reduction in binding to ubiquitin^{Phospho-Ser65} compared to wild-type (WT) Parkin. Isothermal calorimetry analysis of Parkin WT (left), K151A mutant (middle) and H302A mutant (right) with ubiquitin^{Phospho-Ser65}.
2. Table showing the K_d values (in μM), ΔH values (in kcal/mol), ΔS values (in kcal/mol deg) and −TΔS (in kcal/mol) derived from the graphs. Data are representative of two independent experiments.