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

Author

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  • Mizuho Kajikawa

    (Showa Pharmaceutical University, Machida
    Kyushu University)

  • Toyoyuki Ose

    (Faculty of Pharmaceutical Sciences, Hokkaido University)

  • Yuko Fukunaga

    (Kyushu University)

  • Yuki Okabe

    (Kyushu University
    Faculty of Pharmaceutical Sciences, Hokkaido 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
    Faculty of Pharmaceutical Sciences, Hokkaido University)

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.

Suggested Citation

  • Mizuho Kajikawa & Toyoyuki Ose & Yuko Fukunaga & Yuki Okabe & Naoki Matsumoto & Kento Yonezawa & Nobutaka Shimizu & Simon Kollnberger & Masanori Kasahara & Katsumi Maenaka, 2018. "Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06797-8
    DOI: 10.1038/s41467-018-06797-8
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