The structure and binding mode of interleukin-18 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-10-05

AUTHORS

Zenichiro Kato, JunGoo Jee, Hiroaki Shikano, Masaki Mishima, Izuru Ohki, Hidenori Ohnishi, Ailian Li, Kazuyuki Hashimoto, Eiji Matsukuma, Kentaro Omoya, Yutaka Yamamoto, Teruyo Yoneda, Takane Hara, Naomi Kondo, Masahiro Shirakawa

ABSTRACT

Interleukin-18 (IL-18), a cytokine formerly known as interferon-γ- (IFN-γ-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-γ production, Fas-mediated cytotoxicity and developmental regulation of T-lymphocyte helper type I. We determined the solution structure of IL-18 as a first step toward understanding its receptor activation mechanism. It folds into a β-trefoil structure that resembles that of IL-1. Extensive mutagenesis revealed the presence of three sites that are important for receptor activation: two serve as binding sites for IL-18 receptor α (IL-18Rα), located at positions similar to those of IL-1 for IL-1 receptor type I (IL-1RI), whereas the third site may be involved in IL-18 receptor β (IL-18Rβ) binding. The structure and mutagenesis data provide a basis for understanding the IL-18-induced heterodimerization of receptor subunits, which is necessary for receptor activation. More... »

PAGES

966-971

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb993

DOI

http://dx.doi.org/10.1038/nsb993

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041513834

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/14528293


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