3WO3
Crystal structure of IL-18 in complex with IL-18 receptor alpha
Summary for 3WO3
Entry DOI | 10.2210/pdb3wo3/pdb |
Related | 3WO2 3WO4 |
Descriptor | Interleukin-18, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (14 entities in total) |
Functional Keywords | binary complex, beta trefoil fold (ligand), three immunoglobulin-like domains (receptor), immunity, inflammation, autoimmunity, allergy, interleukin-18 receptor beta, glycosylation, serum, membrane, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 12 |
Total formula weight | 346959.29 |
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: 2024-10-30) |
Primary citation | Tsutsumi, 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: 25500532DOI: 10.1038/ncomms6340 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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