Journal
FEBS LETTERS
Volume 588, Issue 21, Pages 3838-3843Publisher
WILEY
DOI: 10.1016/j.febslet.2014.09.019
Keywords
Interleukin 18; Interleukin 18 receptor; Ligand-receptor recognition; X-ray structure
Funding
- Ministry of Science and Technology of China [2011CB910502, 2010CB912402]
- Tsinghua University Initiative Scientific Program
- Toward World-Class University Project of National Tsing Hua University
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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-18R alpha and accessory receptor IL-18R beta. Here we report the crystal structure of IL-18 with the ectodomain of IL-18R alpha, 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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