Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.
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O'Callaghan CA, Tormo J, Willcox BE, Braud VM, Jakobsen BK, Stuart DI, McMichael AJ, Bell JI, Jones EY
Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.
Mol Cell. 1998 Mar;1(4):531-41. doi: 10.1016/s1097-2765(00)80053-2.
- PubMed ID
- 9660937 [ View in PubMed]
- 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.