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is a nonclassical MHC class I (MHCI) molecule that can suppress a wide range of immune responses in the maternal-fetal interface. The human inhibitory immune receptors leukocyte Ig-like receptor (LILR) B1 [also called LIR1, Ig-like transcript 2 (ILT2), or CD85j] and LILRB2 (LIR2/ILT4/CD85d) preferentially recognize HLA-G. HLA-G inherently exhibits various forms, including beta(2)-microglobulin (beta(2)m)-free and disulfide-linked dimer forms. Notably, LILRB1 cannot recognize the beta(2)m-free form of HLA-G or HLA-B27, but LILRB2 can recognize the beta(2)m-free form of HLA-B27. To date, the structural basis for HLA-G/LILR recognition remains to be examined. Here, we report the 2.5-A resolution crystal structure of the LILRB2/HLA-G complex. LILRB2 exhibits an overlapping but distinct MHCI recognition mode compared with LILRB1 and dominantly recognizes the hydrophobic site of the HLA-G alpha3 domain. NMR binding studies also confirmed these LILR recognition differences on both conformed (heavy chain/peptide/beta(2)m) and free forms of beta(2)m. Binding studies using beta(2)m-free MHCIs revealed differential beta(2)m-dependent LILR-binding specificities. These results suggest that subtle structural differences between LILRB family members cause the distinct binding specificities to various forms of HLA-G and other MHCIs, which may in turn regulate immune suppression.","bibjson":{"author":[{"initials":"M","lastname":"Shiroishi","name":"Shiroishi M"},{"initials":"K","lastname":"Kuroki","name":"Kuroki K"},{"initials":"L","lastname":"Rasubala","name":"Rasubala L"},{"initials":"K","lastname":"Tsumoto","name":"Tsumoto K"},{"initials":"I","lastname":"Kumagai","name":"Kumagai I"},{"initials":"E","lastname":"Kurimoto","name":"Kurimoto E"},{"initials":"K","lastname":"Kato","name":"Kato K"},{"initials":"D","lastname":"Kohda","name":"Kohda D"},{"initials":"K","lastname":"Maenaka","name":"Maenaka K"}],"identifier":[{"id":"10.1073/pnas.0605228103","type":"doi"},{"id":"17056715","type":"pubmed"}],"issue":["44"],"journal":{"iso_abbreviation":"Proc. Natl. Acad. Sci. U.S.A.","name":""},"pages":["16412-7"],"title":"Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d).","type":"article","url":"https://pnas.org/doi/full/10.1073/pnas.0605228103","volume":["103"],"year":[2006]},"in_pmc":"N","in_pmce":"Y","open_access":"N"},"resolution":"2.50","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/2dyp"},"rcsb":{"url":"https://www.rcsb.org/structure/2dyp"}},"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\" with LIR-2 NK receptor at 2.50Å resolution","unique_chain_count":4}}