8D7E
Cryo-EM structure of human CNTFR alpha in complex with the Fab fragments of two antibodies
Summary for 8D7E
Entry DOI | 10.2210/pdb8d7e/pdb |
EMDB information | 27228 |
Descriptor | Ciliary neurotrophic factor receptor subunit alpha, H4H25311P2 antibody Fab fragment light chain, H4H25311P2 antibody Fab fragment heavy chain, ... (6 entities in total) |
Functional Keywords | cytokine signaling, cntfr alpha, cytokine, antibody, fab, cytokine-immune system complex, cytokine/immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 5 |
Total formula weight | 135206.47 |
Authors | Zhou, Y.,Franklin, M.C. (deposition date: 2022-06-07, release date: 2023-03-29, Last modification date: 2024-11-06) |
Primary citation | Zhou, Y.,Stevis, P.E.,Cao, J.,Saotome, K.,Wu, J.,Glatman Zaretsky, A.,Haxhinasto, S.,Yancopoulos, G.D.,Murphy, A.J.,Sleeman, M.W.,Olson, W.C.,Franklin, M.C. Structural insights into the assembly of gp130 family cytokine signaling complexes. Sci Adv, 9:eade4395-eade4395, 2023 Cited by PubMed Abstract: 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. PubMed: 36930708DOI: 10.1126/sciadv.ade4395 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.93 Å) |
Structure validation
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