2014年12月
The structural basis for receptor recognition of human interleukin-18
NATURE COMMUNICATIONS
- 巻
- 5
- 号
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1038/ncomms6340
- 出版者・発行元
- NATURE PUBLISHING GROUP
Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation. The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease. IL-18 forms a signalling complex with the IL-18 receptor alpha (R alpha) and beta (R beta) chains at the plasma membrane, which induces multiple inflammatory cytokines. Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains. Generally, the receptors' recognition mode for IL-18 is similar to IL-1 beta; however, certain notable differences were observed. The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode. The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
- リンク情報
-
- DOI
- https://doi.org/10.1038/ncomms6340
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000347220300001&DestApp=WOS_CPL
- URL
- http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84923278457&origin=inward
- ID情報
-
- DOI : 10.1038/ncomms6340
- ISSN : 2041-1723
- Web of Science ID : WOS:000347220300001