Fig. 1: Cryo-EM structures of the RXFP4-Gi complexes. | Nature Communications

Fig. 1: Cryo-EM structures of the RXFP4-Gi complexes.

From: Ligand recognition mechanism of the human relaxin family peptide receptor 4 (RXFP4)

Fig. 1

a–c Cryo-EM density maps (left panel) and cartoon representation (middle) of the INSL5−RXFP4−Gi−scFv16 complex (a), compound 4−RXFP4−Gi−scFv16 complex (b) and DC591053−RXFP4−Gi−scFv16 complex (c). Atomic models and EM densities of the three ligands are shown as sticks and surfaces, respectively. The A chain of INSL5 is shown in forest green and the B chain in light green, compound 4 in cyan and DC591053 in magenta. The corresponding RXFP4 is shown in orange, dark sea green and medium purple, respectively. Gαi in salmon, Gβ in cornflower blue, Gγ in light sea green, and scFv16 in dark gray. d Activities of INSL5 and DC591053 in RXFP4 and cross-reactivity of compound 4 in RXFP3 and RXFP4. The thickness of lines indicates the strength of affinity. e INSL5, compound 4 and DC591053 induced cAMP signaling in cells expressing wild-type RXFP4. Data shown are means ± S.E.M. of three independent experiments (n = 3) performed in quadruplicate. Source data are provided as a Source Data file.

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