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is a nonclassical major histocompatibility complex class I (MHCI) molecule, which is expressed in trophoblasts and confers immunological tolerance in the maternal-fetal interface by binding to leukocyte Ig-like receptors (LILRs, also called as LIR/ILT/CD85) and CD8. HLA-G is expressed in disulfide-linked dimer form both in solution and at the cell surface. Interestingly, MHCI dimer formations have been involved in pathogenesis and T cell activation. The structure and receptor binding characteristics of MHCI dimers have never been evaluated. Here we performed binding studies showing that the HLA-G dimer exhibited higher overall affinity to LILRB1/2 than the monomer by significant avidity effects. Furthermore, the cell reporter assay demonstrated that the dimer formation remarkably enhanced the LILRB1-mediated signaling at the cellular level. We further determined the crystal structure of the wild-type dimer of HLA-G with the intermolecular Cys(42)-Cys(42) disulfide bond. This dimer structure showed the oblique configuration to expose two LILR/CD8-binding sites upward from the membrane easily accessible for receptors, providing plausible 1:2 (HLA-G dimer:receptors) complex models. These results indicated that the HLA-G dimer conferred increased avidity in a proper structural orientation to induce efficient LILR signaling, resulting in the dominant immunosuppressive effects. Moreover, structural and functional implications for other MHCI dimers observed in activated T cells and the pathogenic allele, HLA-B27, are discussed.","bibjson":{"author":[{"initials":"M","lastname":"Shiroishi","name":"Shiroishi M"},{"initials":"K","lastname":"Kuroki","name":"Kuroki K"},{"initials":"T","lastname":"Ose","name":"Ose T"},{"initials":"L","lastname":"Rasubala","name":"Rasubala L"},{"initials":"I","lastname":"Shiratori","name":"Shiratori I"},{"initials":"H","lastname":"Arase","name":"Arase H"},{"initials":"K","lastname":"Tsumoto","name":"Tsumoto K"},{"initials":"I","lastname":"Kumagai","name":"Kumagai I"},{"initials":"D","lastname":"Kohda","name":"Kohda D"},{"initials":"K","lastname":"Maenaka","name":"Maenaka K"}],"identifier":[{"id":"10.1074/jbc.M512305200","type":"doi"},{"id":"16455647","type":"pubmed"}],"issue":["15"],"journal":{"iso_abbreviation":"J. Biol. Chem.","name":""},"pages":["10439-47"],"title":"Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimer.","type":"article","url":"https://www.sciencedirect.com/science/article/abs/pii/S0021925819563979","volume":["281"],"year":[2006]},"in_pmc":"N","in_pmce":"N","open_access":"N"},"resolution":"3.20","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/2d31"},"rcsb":{"url":"https://www.rcsb.org/structure/2d31"}},"species":{"common_name":"Human","match_type":"histo:assign_species","scientific_name":"Homo sapiens","slug":"homo_sapiens"},"tcr":null,"title":"HLA-G*01:01 binding \"RIIPRHLQL\" at 3.20Å resolution","unique_chain_count":3}}