6A97
Crystal structure of MHC-like MILL2
Summary for 6A97
| Entry DOI | 10.2210/pdb6a97/pdb |
| Descriptor | MHC I-like leukocyte 2 long form, Beta-2-microglobulin, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | mhc-like, immune system |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 89623.71 |
| Authors | Kajikawa, M.,Ose, T.,Maenaka, K. (deposition date: 2018-07-11, release date: 2018-12-05, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 30337538DOI: 10.1038/s41467-018-06797-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.148 Å) |
Structure validation
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