1J0S

Solution structure of the human interleukin-18

Summary for 1J0S

• Entry DOI: 10.2210/pdb1j0s/pdb
• Descriptor: Interleukin-18 (1 entity in total)
• Functional Keywords: beta trefoil, cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q14116
• Total number of polymer chains: 1
• Total formula weight: 18239.73

Authors

Kato, Z.,Jee, J.,Shikano, H.,Mishima, M.,Ohki, I.,Yoneda, T.,Hara, T.,Torigoe, K.,Kondo, N.,Shirakawa, M. (deposition date: 2002-11-21, release date: 2003-11-11, Last modification date: 2023-12-27)

Primary citation

Kato, Z.,Jee, J.,Shikano, H.,Mishima, M.,Ohki, I.,Ohnishi, H.,Li, A.,Hashimoto, K.,Matsukuma, E.,Omoya, K.,Yamamoto, Y.,Yoneda, T.,Hara, T.,Kondo, N.,Shirakawa, M.
The structure and binding mode of interleukin-18
Nat.Struct.Biol., 10:966-971, 2003

PubMed Abstract: Interleukin-18 (IL-18), a cytokine formerly known as interferon-gamma- (IFN-gamma-) inducing factor, has pleiotropic immunoregulatory functions, including augmentation of IFN-gamma 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 beta-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 alpha (IL-18Ralpha), 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 beta (IL-18Rbeta) 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.

PubMed: 14528293
DOI: 10.1038/nsb993

Experimental method

SOLUTION NMR