Fig. 3
From: A multi-lock inhibitory mechanism for fine-tuning enzyme activities of the HECT family E3 ligases
WW2L34-HECT interface. a The detailed structures of the WW2-HECT, L-HECT, and WW4-HECT interfaces from 2L34HECT and L34HECT. b–d GST pull-down assay of GST-tagged WWP1 WW12L34 (referred to as WW) with Trx-HECT. The mutations were predicted to impair interactions involving the “Re” site in WW2-HECT (M627EHECT and W409AWW2), the “Le” site in WW4-HECT (Y543AHECT and H517AWW4) or the “H” site in L-HECT (F617EHECT). e Statistical results of the autoubiquitination assay of Trx-tagged WT WWP1 12L34HECT and mutants in Supplementary Fig. 2. The mutations were located in the WW2L34-HECT-binding interface. Data are presented as the mean ± SD of triplicate experiments. Source data are provided as a Source Data file
