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8D7E

Cryo-EM structure of human CNTFR alpha in complex with the Fab fragments of two antibodies

Summary for 8D7E
Entry DOI10.2210/pdb8d7e/pdb
EMDB information27228
DescriptorCiliary neurotrophic factor receptor subunit alpha, H4H25311P2 antibody Fab fragment light chain, H4H25311P2 antibody Fab fragment heavy chain, ... (6 entities in total)
Functional Keywordscytokine signaling, cntfr alpha, cytokine, antibody, fab, cytokine-immune system complex, cytokine/immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains5
Total formula weight135206.47
Authors
Zhou, Y.,Franklin, M.C. (deposition date: 2022-06-07, release date: 2023-03-29, Last modification date: 2024-11-06)
Primary citationZhou, 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: 36930708
DOI: 10.1126/sciadv.ade4395
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.93 Å)
Structure validation

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