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3WO4

Crystal structure of the IL-18 signaling ternary complex

Summary for 3WO4
Entry DOI10.2210/pdb3wo4/pdb
Related3WO2 3WO3
DescriptorInterleukin-18, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (12 entities in total)
Functional Keywordsternary complex, beta trefoil fold (ligand), three immunoglobulin-like domains (receptors), immunity, inflammation, autoimmunity, allergy, glycosylation, serum, membrane, immune system
Biological sourceHomo sapiens (human)
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Total number of polymer chains3
Total formula weight98472.25
Authors
Tsutsumi, N.,Kimura, T.,Arita, K.,Ariyoshi, M.,Ohnishi, H.,Kondo, N.,Shirakawa, M.,Kato, Z.,Tochio, H. (deposition date: 2013-12-19, release date: 2014-12-17, Last modification date: 2024-11-20)
Primary citationTsutsumi, N.,Kimura, T.,Arita, K.,Ariyoshi, M.,Ohnishi, H.,Yamamoto, T.,Zuo, X.,Maenaka, K.,Park, E.Y.,Kondo, N.,Shirakawa, M.,Tochio, H.,Kato, Z.
The structural basis for receptor recognition of human interleukin-18
Nat Commun, 5:5340-5340, 2014
Cited by
PubMed Abstract: Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation. The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease. IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines. Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains. Generally, the receptors' recognition mode for IL-18 is similar to IL-1β; however, certain notable differences were observed. The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode. The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
PubMed: 25500532
DOI: 10.1038/ncomms6340
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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