Fig. 5: Structural and functional analysis of the HOIL-1 and RNF216 RING2/E2-Ub interfaces. | Nature Communications

Fig. 5: Structural and functional analysis of the HOIL-1 and RNF216 RING2/E2-Ub interfaces.

From: The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family

Fig. 5: Structural and functional analysis of the HOIL-1 and RNF216 RING2/E2-Ub interfaces.The alternative text for this image may have been generated using AI.

a Binding of the UbcH7-Ub isopeptide conjugate to the HOIL-1 RING2 (dark green) and preceding helix (IBR-RING2 helix, light green) via the Ub I44 hydrophobic patch (pink). b Binding of the UbcH7-Ub isopeptide conjugate to the RNF216 RING2 (dark blue) and preceding helix (IBR-RING2 helix, light blue). Ub (pink) forms extensive interactions with polar and non-polar residues in the RING2 and IBR-RING2 helix. c Time-course of HOIL-1 catalysed E2-Ub discharge assay with WT HOIL-1 and IBR-RING2 mutants. The right panel shows quantification of three independent experiments. Source data are provided as a Source data file.

Back to article page