The structural basis for receptor recognition of human interleukin-18
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. Furthermore, the structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
- Authors:
-
- 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)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1221149
- Alternate Identifier(s):
- OSTI ID: 1241361
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 5; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; biological sciences; biochemistry; immunology
Citation Formats
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, and Kato, Zenichiro. The structural basis for receptor recognition of human interleukin-18. United States: N. p., 2014.
Web. doi:10.1038/ncomms6340.
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. The structural basis for receptor recognition of human interleukin-18. United States. https://doi.org/10.1038/ncomms6340
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, and Kato, Zenichiro. Mon .
"The structural basis for receptor recognition of human interleukin-18". United States. https://doi.org/10.1038/ncomms6340. https://www.osti.gov/servlets/purl/1221149.
@article{osti_1221149,
title = {The structural basis for receptor recognition of human interleukin-18},
author = {Tsutsumi, Naotaka and Kimura, Takeshi and Arita, Kyohei and Ariyoshi, Mariko and Ohnishi, Hidenori and Yamamoto, Takahiro and Zuo, Xiaobing and Maenaka, Katsumi and Park, Enoch Y. and Kondo, Naomi and Shirakawa, Masahiro and Tochio, Hidehito and Kato, Zenichiro},
abstractNote = {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.},
doi = {10.1038/ncomms6340},
journal = {Nature Communications},
number = ,
volume = 5,
place = {United States},
year = {Mon Dec 15 00:00:00 EST 2014},
month = {Mon Dec 15 00:00:00 EST 2014}
}
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