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

O'Callaghan CA, Tormo J, Willcox BE, Braud VM, Jakobsen BK, Stuart DI, McMichael AJ, Bell JI, Jones EY
Mol Cell 1 531-41 (1998)
Cited: 127 times
EuropePMC logo PMID: 9660937

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.

Reviews - 1mhe mentioned but not cited (2)

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  5. Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes. Walters LC, Rozbesky D, Harlos K, Quastel M, Sun H, Springer S, Rambo RP, Mohammed F, Jones EY, McMichael AJ, Gillespie GM. Cell Rep 39 110959 (2022)
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Reviews citing this publication (43)

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Articles citing this publication (75)

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Related citations provided by authors (1)

  1. Production, Crystallization, and Preliminary X-Ray Analysis of the Human Mhc Class Ib Molecule Hla-E. O'Callaghan CA, Tormo J, Willcox BE, Blundell CD, Jakobsen BK, Stuart DI, Mcmichael AJ, Bell JI, Jones EY Protein Sci. 7 1264- (1998)

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