Fig. 5: Different conformational states of ZNRF3 in various assemblies of the LGR4-RSPO2(Fu)-ZNRF3 complexes. | Nature Communications

Fig. 5: Different conformational states of ZNRF3 in various assemblies of the LGR4-RSPO2(Fu)-ZNRF3 complexes.

From: Structural insights into the LGR4-RSPO2-ZNRF3 complexes regulating WNT/β-catenin signaling

Fig. 5

a ZNRF3 in the heterotrimer: the linker between the extracellular domain of ZNRF3 and TM helix is absent. b ZNRF3 in pentamer A: one of the TM helices in the ZNRF3 dimer is completely missing, and the linker between the extracellular domain and the TM helix is also absent. c ZNRF3 in pentamer B: the two TM helices exhibit a “finger-crossed” arrangement. d ZNRF3 in the di-heterotrimer: the two TM helices adopt an inverted V-shaped configuration. ZNRF3 is depicted in purple or orange.

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