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Solution Structures of Cytosolic RNA Sensor MDA5 and LGP2 C-terminal Domains : Identification of the RNA Recognition Loop in RIG-I-LIKE Receptors

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タイトル: Solution Structures of Cytosolic RNA Sensor MDA5 and LGP2 C-terminal Domains : Identification of the RNA Recognition Loop in RIG-I-LIKE Receptors
著者: Takahasi, Kiyohiro 著作を一覧する
Kumeta, Hiroyuki 著作を一覧する
Tsuduki, Natsuko 著作を一覧する
Narita, Ryo 著作を一覧する
Shigemoto, Taeko 著作を一覧する
Hirai, Reiko 著作を一覧する
Yoneyama, Mitsutoshi 著作を一覧する
Horiuchi, Masataka 著作を一覧する
Ogura, Kenji 著作を一覧する
Fujita, Takashi 著作を一覧する
Inagaki, Fuyuhiko 著作を一覧する
発行日: 2009年 6月26日
出版者: American Society for Biochemistry and Molecular Biology
誌名: Journal of Biological Chemistry
巻: 284
号: 26
開始ページ: 17465
終了ページ: 17474
出版社 DOI: 10.1074/jbc.M109.007179
抄録: The RIG-I like receptor (RLR) comprises three homologues: RIG-I (retinoic acid-inducible gene I), MDA5(melanoma differentiation-associated gene 5), and LGP2 (laboratory of genetics and physiology 2). Each RLR senses different viral infections by recognizing replicating viral RNA in the cytoplasm. The RLR contains a conserved C-terminal domain (CTD), which is responsible for the binding specificity to the viral RNAs, including double-stranded RNA (dsRNA) and 5'-triphosphated single-stranded RNA (5'ppp-ssRNA). Here, the solution structures of the MDA5 and LGP2 CTD domains were solved by NMR and compared with those of RIG-I CTD. The CTD domains each have a similar fold and a similar basic surface but there is the distinct structural feature of a RNA binding loop; The LGP2 and RIG-I CTD domains have a large basic surface, one bank of which is formed by the RNA binding loop. MDA5 also has a large basic surface that is extensively flat due to open conformation of the RNA binding loop. The NMR chemical shift perturbation study showed that dsRNA and 5'ppp-ssRNA are bound to the basic surface of LGP2 CTD, whereas dsRNA is bound to the basic surface of MDA5 CTD but much more weakly, indicating that the conformation of the RNA binding loop is responsible for the sensitivity to dsRNA and 5'ppp-ssRNA. Mutation study of the basic surface and the RNA binding loop supports the conclusion from the structure studies. Thus, the CTD is responsible for the binding affinity to the viral RNAs.
Rights: © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
資料タイプ: article
URI: http://hdl.handle.net/2115/38780
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 稲垣 冬彦

 

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