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

Mizuho Kajikawa, Toyoyuki Ose, Yuko Fukunaga, Yuki Okabe, Naoki Matsumoto, Kento Yonezawa, Nobutaka Shimizu, Simon Kollnberger, Masanori Kasahara and Katsumi Maenaka ()
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Mizuho Kajikawa: Showa Pharmaceutical University, Machida
Toyoyuki Ose: Faculty of Pharmaceutical Sciences, Hokkaido University
Yuko Fukunaga: Kyushu University
Yuki Okabe: Kyushu University
Naoki Matsumoto: Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa
Kento Yonezawa: High Energy Accelerator Research Organization, Tsukuba
Nobutaka Shimizu: High Energy Accelerator Research Organization, Tsukuba
Simon Kollnberger: University of Cardiff, Henry Wellcome Building, Heath Park
Masanori Kasahara: Faculty of Medicine and Graduate School of Medicine, Hokkaido University
Katsumi Maenaka: Kyushu University

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: 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 Å resolution, revealing an organization similar to classical MHC class I. However, the α1-α2 domains are not tightly fixed on the α3-β2m domains, indicating unusual interdomain flexibility. The groove between the two helices in the α1-α2 domains is too narrow to permit ligand binding. Notably, an unusual basic patch on the α3 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.

Date: 2018
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DOI: 10.1038/s41467-018-06797-8

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