白细胞介素6（IL-6）家族的细胞因子通过gp130受体的同源二聚化或者与第二信号受体的异源二聚至关重要，在各个细胞进程中发挥着关键作用。我们测定了这个家族五个信号复合物的低温电子显微镜结构，这些复合物包括全长受体外区被它们各自的配体（纤毛神经营养因子、类心肌细胞因子因子1（CLCF1）、白血病抑制因子、IL-27和IL-6）结合。我们的结构共同揭示了这些复合物的组装中的相似性和不同之处。所有复合物中信号受体的急弯将膜近端区域带到约30埃的范围内，但是又具有着不同的距离和方向。我们还揭示了CLCF1如何与其分泌辅助因子细胞因子受体样因子1发生联系。我们的数据为治疗上治疗gp130介导的信号提供了有价值的见解。

The interleukin-6 (IL-6) family cytokines signal through gp130 receptor homodimerization or heterodimerization with a second signaling receptor and play crucial roles in various cellular processes. We determined cryo-electron microscopy structures of five signaling complexes of this family, containing full receptor ectodomains bound to their respective ligands ciliary neurotrophic factor, cardiotrophin-like cytokine factor 1 (CLCF1), leukemia inhibitory factor, IL-27, and IL-6. Our structures collectively reveal similarities and differences in the assembly of these complexes. The acute bends at both signaling receptors in all complexes bring the membrane-proximal domains to a ~30 angstrom range but with distinct distances and orientations. We also reveal how CLCF1 engages its secretion chaperone cytokine receptor-like factor 1. Our data provide valuable insights for therapeutically targeting gp130-mediated signaling.