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primary function of the monomorphic MHC class Ib molecule Qa-1(b) is to present peptides derived from the leader sequences of other MHC class I molecules for recognition by the CD94-NKG2 receptors expressed by NK and T cells. Whereas the mode of peptide presentation by its ortholog HLA-E, and subsequent recognition by CD94-NKG2A, is known, the molecular basis of Qa-1(b) function is unclear. We have assessed the interaction between Qa-1(b) and CD94-NKG2A and shown that they interact with an affinity of 17 \u03bcM. Furthermore, we have determined the structure of Qa-1(b) bound to the leader sequence peptide, Qdm (AMAPRTLLL), to a resolution of 1.9 \u00c5 and compared it with that of HLA-E. The crystal structure provided a basis for understanding the restricted peptide repertoire of Qa-1(b). Whereas the Qa-1(b-AMAPRTLLL) complex was similar to that of HLA-E, significant sequence and structural differences were observed between the respective Ag-binding clefts. However, the conformation of the Qdm peptide bound by Qa-1(b) was very similar to that of peptide bound to HLA-E. Although a number of conserved innate receptors can recognize heterologous ligands from other species, the structural differences between Qa-1(b) and HLA-E manifested in CD94-NKG2A ligand recognition being species specific despite similarities in peptide sequence and conformation. Collectively, our data illustrate the structural homology between Qa-1(b) and HLA-E and provide a structural basis for understanding peptide repertoire selection and the specificity of the interaction of Qa-1(b) with CD94-NKG2 receptors.","bibjson":{"author":[{"initials":"L","lastname":"Zeng","name":"Zeng L"},{"initials":"LC","lastname":"Sullivan","name":"Sullivan LC"},{"initials":"JP","lastname":"Vivian","name":"Vivian JP"},{"initials":"NG","lastname":"Walpole","name":"Walpole NG"},{"initials":"CM","lastname":"Harpur","name":"Harpur CM"},{"initials":"J","lastname":"Rossjohn","name":"Rossjohn J"},{"initials":"CS","lastname":"Clements","name":"Clements CS"},{"initials":"AG","lastname":"Brooks","name":"Brooks AG"}],"identifier":[{"id":"10.4049/jimmunol.1102379","type":"doi"},{"id":"22131332","type":"pubmed"}],"issue":["1"],"journal":{"iso_abbreviation":"J. Immunol.","name":""},"pages":["302-10"],"title":"A structural basis for antigen presentation by the MHC class Ib molecule, Qa-1b.","type":"article","url":"http://www.jimmunol.org/lookup/doi/10.4049/jimmunol.1102379","volume":["188"],"year":[2012]},"in_pmc":"N","in_pmce":"N","open_access":"N"},"resolution":"1.90","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/3vj6"},"rcsb":{"url":"https://www.rcsb.org/structure/3vj6"}},"species":{"common_name":"Mouse","match_type":"histo:assign_species","scientific_name":"Mus musculus","slug":"mus_musculus"},"tcr":null,"title":"Qa-1b binding \"AMAPRTLLL\" at 1.90Å resolution","unique_chain_count":3}}