Structural basis for the specific recognition of IL-18 by its alpha receptor |
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| Authors: | Hui Wei Dongli Wang Yun Qian Xi Liu Shilong Fan Hsien-Sheng Yin Xinquan Wang |
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| Institution: | 1. Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing 100084, China;2. Collaborative Innovation Center for Biotherapy, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, Chengdu, China;3. Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan |
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| Abstract: | Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses. It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ. Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition. It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family. We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family. |
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| Keywords: | Interleukin 18 Interleukin 18 receptor Ligand-receptor recognition X-ray structure |
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