HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

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

This item is licensed under:Creative Commons Attribution 4.0 International

Files in This Item:
WoS_86357_Maenaka.pdf1.32 MBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility
Authors: Kajikawa, Mizuho Browse this author
Ose, Toyoyuki Browse this author
Fukunaga, Yuko Browse this author
Okabe, Yuki Browse this author
Matsumoto, Naoki Browse this author
Yonezawa, Kento Browse this author
Shimizu, Nobutaka Browse this author
Kollnberger, Simon Browse this author
Kasahara, Masanori Browse this author
Maenaka, Katsumi Browse this author →KAKEN DB
Issue Date: 18-Oct-2018
Publisher: Nature Publishing Group
Journal Title: Nature communications
Volume: 9
Start Page: 4330
Publisher DOI: 10.1038/s41467-018-06797-8
Abstract: 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.
Type: article
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 前仲 勝実

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University