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Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility


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タイトル: Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
著者: Kajikawa, Mizuho 著作を一覧する
Ose, Toyoyuki 著作を一覧する
Fukunaga, Yuko 著作を一覧する
Okabe, Yuki 著作を一覧する
Matsumoto, Naoki 著作を一覧する
Yonezawa, Kento 著作を一覧する
Shimizu, Nobutaka 著作を一覧する
Kollnberger, Simon 著作を一覧する
Kasahara, Masanori 著作を一覧する
Maenaka, Katsumi 著作を一覧する
発行日: 2018年10月18日
出版者: Nature Publishing Group
誌名: Nature communications
巻: 9
開始ページ: 4330
出版社 DOI: 10.1038/s41467-018-06797-8
抄録: The MILL family, composed of MILL1 and MILL2, is a group of nonclassical MHC class I molecules that occur in some orders of mammals. It has been reported that mouse MILL2 is involved in wound healing; however, the molecular mechanisms remain unknown. Here, we determine the crystal structure of MILL2 at 2.15 angstrom resolution, revealing an organization similar to classical MHC class I. However, the alpha 1-alpha 2 domains are not tightly fixed on the alpha 3-beta 2m domains, indicating unusual interdomain flexibility. The groove between the two helices in the alpha 1-alpha 2 domains is too narrow to permit ligand binding. Notably, an unusual basic patch on the alpha 3 domain is involved in the binding to heparan sulfate which is essential for MILL2 interactions with fibroblasts. These findings suggest that MILL2 has a unique structural architecture and physiological role, with binding to heparan sulfate proteoglycans on fibroblasts possibly regulating cellular recruitment in biological events.
資料タイプ: article
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 前仲 勝実


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