Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.

C A O'Callaghan; J Tormo; B E Willcox; V M Braud; B K Jakobsen; D I Stuart; A J McMichael; J I Bell; E Y Jones

doi:10.1016/s1097-2765(00)80053-2

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Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.

C A O'Callaghan·J Tormo·B E Willcox·V M Braud·B K Jakobsen·D I Stuart·A J McMichael·J I Bell·E Y Jones

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Abstract

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.

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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 HLA-E Antigens Journal Article Research Support, Non-U.S. Gov't

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C A O'Callaghan, J Tormo, B E Willcox, V M Braud, B K Jakobsen, D I Stuart, A J McMichael, J I Bell, E Y Jones. 1998. Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.. https://doi.org/10.1016/s1097-2765(00)80053-2

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