Fig. 5: An E6-binding pocket in E6AP.
From: Structural insights into the functional mechanism of the ubiquitin ligase E6AP
a E6 (cartoon, red) binds into a pocket in E6AP (surface, green). b Zoomed-in view of the interaction between E6 and the E6-binding pocket in E6AP. The E6-binding pocket, depicted as a lipophilicity potential surface (hydrophobic, gold; hydrophilic, cyan), is formed by the α1-helix of the N-lobe, the tower, and the loop-helix-loop element. c–e Detailed interactions in the corresponding area outlined by the colored boxes in b. f Effect of E6AP mutations on ubiquitination of the substrate p53. The mutations are at the E6/E6-binding pocket binding interface. The activity of E6AP toward p53 is negatively correlated with the amount of unmodified p53. g Statistics of the enzymatic activity in f. Statistical significance tests were performed to compare the amount of unmodified p53 by the wildtype and mutant E6AP at each time point. Data are presented as the mean ± SD of triplicate experiments. ****p < 0.0001 based on one-way analysis of variance (ANOVA) with Tukey’s multiple comparison test. Source data are provided as a Source Data file.
