3WO2

Crystal structure of human interleukin-18

Summary for 3WO2

• Entry DOI: 10.2210/pdb3wo2/pdb
• Related: 3WO3 3WO4
• Descriptor: Interleukin-18, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta trefoil fold, il-1 superfamily, immunity, inflammation, autoimmunity, allergy, interleukin-18 receptor alpha, interleukin-18 receptor beta, serum, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q14116
• Total number of polymer chains: 4
• Total formula weight: 80721.68

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: 2023-11-08)

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

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

Experimental method

X-RAY DIFFRACTION (2.33 Å)