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is a nonclassical major histocompatibility complex class I (MHC-I) molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the maternal immune response. HLA-G binds a limited repertoire of peptides and interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2 and possibly with certain natural killer cell receptors. To gain further insights into HLA-G function, we determined the 1.9-A structure of a monomeric HLA-G complexed to a natural endogenous peptide ligand from histone H2A (RIIPRHLQL). An extensive network of contacts between the peptide and the antigen-binding cleft reveal a constrained mode of binding reminiscent of the nonclassical HLA-E molecule, thereby providing a structural basis for the limited peptide repertoire of HLA-G. The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands. The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.","bibjson":{"author":[{"initials":"CS","lastname":"Clements","name":"Clements CS"},{"initials":"L","lastname":"Kjer-Nielsen","name":"Kjer-Nielsen L"},{"initials":"L","lastname":"Kostenko","name":"Kostenko L"},{"initials":"HL","lastname":"Hoare","name":"Hoare HL"},{"initials":"MA","lastname":"Dunstone","name":"Dunstone MA"},{"initials":"E","lastname":"Moses","name":"Moses E"},{"initials":"K","lastname":"Freed","name":"Freed K"},{"initials":"AG","lastname":"Brooks","name":"Brooks AG"},{"initials":"J","lastname":"Rossjohn","name":"Rossjohn J"},{"initials":"J","lastname":"McCluskey","name":"McCluskey J"}],"identifier":[{"id":"10.1073/pnas.0409676102","type":"doi"},{"id":"15718280","type":"pubmed"}],"issue":["9"],"journal":{"iso_abbreviation":"Proc. Natl. Acad. Sci. 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