6A97

Crystal structure of MHC-like MILL2

6A97 の概要

• エントリーDOI: 10.2210/pdb6a97/pdb
• 分子名称: MHC I-like leukocyte 2 long form, Beta-2-microglobulin, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: mhc-like, immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 89623.71

構造登録者

Kajikawa, M.,Ose, T.,Maenaka, K. (登録日: 2018-07-11, 公開日: 2018-12-05, 最終更新日: 2024-11-13)

主引用文献

Kajikawa, M.,Ose, T.,Fukunaga, Y.,Okabe, Y.,Matsumoto, N.,Yonezawa, K.,Shimizu, N.,Kollnberger, S.,Kasahara, M.,Maenaka, K.
Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.
Nat Commun, 9:4330-4330, 2018

PubMed 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-βm 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.

PubMed: 30337538
DOI: 10.1038/s41467-018-06797-8

実験手法

X-RAY DIFFRACTION (2.148 Å)