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Structural basis for the specific recognition of IL‐18 by its alpha receptor
Author(s) -
Wei Hui,
Wang Dongli,
Qian Yun,
Liu Xi,
Fan Shilong,
Yin Hsien-Sheng,
Wang Xinquan
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.019
Subject(s) - ectodomain , receptor , ligand (biochemistry) , regulator , microbiology and biotechnology , innate immune system , complementarity (molecular biology) , biology , chemistry , immunology , biochemistry , genetics , gene
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.