Fig. 3: The rearrangement RING domain in different complexes.
From: Structural insights into the LGR4-RSPO2-ZNRF3 complexes regulating WNT/β-catenin signaling
a Superposition of the map and model of the LGR4-RSPO2-ZNRF3(RING) (1:1:1, heterotrimer, contour level: 2.8σ). b Map of the LGR4-RSPO2-ZNRF3(RING) (1:2:2, pentamer B, contour level: 2.8σ). c Superposition of the map and model of the TM helix and RING domain in pentamer B, shown in the low-pass map (contour level: 4.38σ) from different perspectives. d Map of ZNRF3(RING) in pentamer B (contour level: 5.4σ). e Wnt3a-stimulated-TOPFlash activity regulated by WT or V229-P-S230 mutant of ZNRF3, n = 4, p value = 0.0356. Source data are provided as a Source Data file. f Map of ZNRF3 (ΔRING) in di-heterotrimer (contour level: 11.08σ). g The map of the LGR4-RSPO2-ZNRF3 complex in its di-heterodimer form (2:2:2), with ZNRF3 containing the RING domain. Each value represents the mean ± SEM from four independent experiments.
