The structural basis for receptor recognition of human interleukin-18

Naotaka Tsutsumi, Takeshi Kimura, Kyohei Arita, Mariko Ariyoshi, Hidenori Ohnishi (), Takahiro Yamamoto, Xiaobing Zuo, Katsumi Maenaka, Enoch Y. Park, Naomi Kondo, Masahiro Shirakawa, Hidehito Tochio () and Zenichiro Kato
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Naotaka Tsutsumi: Graduate School of Engineering, Kyoto University
Takeshi Kimura: Graduate School of Medicine, Gifu University
Kyohei Arita: Graduate School of Nanobioscience, Yokohama City University
Mariko Ariyoshi: Graduate School of Engineering, Kyoto University
Hidenori Ohnishi: Graduate School of Medicine, Gifu University
Takahiro Yamamoto: Graduate School of Medicine, Gifu University
Xiaobing Zuo: Argonne National Laboratory
Katsumi Maenaka: Laboratory of Biomolecular Science and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University
Enoch Y. Park: Research Institute of Green Science and Technology, Graduate school of Science and Technology, Shizuoka University
Naomi Kondo: Graduate School of Medicine, Gifu University
Masahiro Shirakawa: Graduate School of Engineering, Kyoto University
Hidehito Tochio: Graduate School of Science, Kyoto University, Kitashirakawa-oiwake, Sakyo-ku
Zenichiro Kato: Graduate School of Medicine, Gifu University

Nature Communications, 2014, vol. 5, issue 1, 1-13

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6340

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