The structural basis for receptor recognition of human interleukin-18

Tsutsumi, Naotaka; Kimura, Takeshi; Arita, Kyohei; Ariyoshi, Mariko; Ohnishi, Hidenori; Yamamoto, Takahiro; Zuo, Xiaobing; Maenaka, Katsumi; Park, Enoch Y.; Kondo, Naomi; Shirakawa, Masahiro; Tochio, Hidehito; Kato, Zenichiro

doi:10.1038/ncomms6340

Title: The structural basis for receptor recognition of human interleukin-18

Journal Article · Mon Dec 15 00:00:00 EST 2014 · Nature Communications

DOI:https://doi.org/10.1038/ncomms6340· OSTI ID:1221149

Tsutsumi, Naotaka ^[1]; Kimura, Takeshi ^[2]; Arita, Kyohei ^[3]; Ariyoshi, Mariko ^[1]; Ohnishi, Hidenori ^[2]; Yamamoto, Takahiro ^[2]; Zuo, Xiaobing ^[4]; Maenaka, Katsumi ^[5]; Park, Enoch Y. ^[6]; Kondo, Naomi ^[2]; Shirakawa, Masahiro ^[7]; Tochio, Hidehito ^[1]; Kato, Zenichiro ^[2]

Kyoto Univ., Kyoto (Japan)
Gifu Univ., Yanagido (Japan)
Yokohama City Univ., Kanagawa (Japan)
Argonne National Lab. (ANL), Argonne, IL (United States)
Hokkaido Univ., Sapporo (Japan)
Shizuoka Univ., Shizuoka (Japan)
Kyoto Univ., Kyoto (Japan); Japan Sciences and Technology Agency, Tokyo (Japan)

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. Furthermore, the structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1221149

Alternate ID(s):: OSTI ID: 1241361

Journal Information:: Nature Communications, Vol. 5; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 78 works

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