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The crystal structure of the nonclassical human class lb MHC molecule HLA-E has been determined in complex with a prototypic ligand, the nonamer peptide (VMAPRTVLL), derived from the highly conserved residues 3-11 of the human MHC class la leader sequence. The mode of peptide binding retains some of the standard features observed in MHC class la complexes, but novel features imply that HLA-E has evolved to mediate specific binding to a tightly defined set of almost identical hydrophobic peptides from the highly conserved class l leader sequences. These molecular adaptations make HLA-E a rigorous checkpoint at the cell surface reporting on the integrity of the antigen processing pathway to CD94/NKG2 receptor-bearing natural killer cells.


Journal article


Mol Cell

Publication Date





531 - 541


Crystallography, HLA Antigens, HLA-B8 Antigen, Histocompatibility Antigens Class I, Humans, Hydrogen Bonding, Peptide Fragments, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary