Structural highlights
Function
[IL18R_HUMAN] Receptor for interleukin 18 (IL-18). Binding to the agonist leads to the activation of NF-kappa-B. [IL18_HUMAN] Augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells.
Publication Abstract from PubMed
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-18Ralpha and accessory receptor IL-18Rbeta. Here we report the crystal structure of IL-18 with the ectodomain of IL-18Ralpha, 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.
Structural basis for the specific recognition of IL-18 by its alpha receptor.,Wei H, Wang D, Qian Y, Liu X, Fan S, Yin HS, Wang X FEBS Lett. 2014 Sep 26. pii: S0014-5793(14)00696-6. doi:, 10.1016/j.febslet.2014.09.019. PMID:25261253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wei H, Wang D, Qian Y, Liu X, Fan S, Yin HS, Wang X. Structural basis for the specific recognition of IL-18 by its alpha receptor. FEBS Lett. 2014 Sep 26. pii: S0014-5793(14)00696-6. doi:, 10.1016/j.febslet.2014.09.019. PMID:25261253 doi:http://dx.doi.org/10.1016/j.febslet.2014.09.019
