The human major histocompatibility complex class Ib molecule HLA‐E binds signal sequence‐derived peptides with primary anchor residues at positions 2 and 9
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Discussion
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Implication
In vitro study demonstrates HLA-E binds MHC class I signal sequence peptides using positions 2 and 9 as primary anchors, highlighting conserved peptide recognition mechanisms across species.
Key Points
- To evaluate the peptide binding specificity of human MHC class Ib molecule HLA-E compared to mouse Qa-1 and define its required peptide anchor residues.
- Developed an in vitro peptide binding assay to directly assess and compare binding specificity between human HLA-E and mouse Qa-1.
- Assayed binding affinity using nonamer signal sequence-derived peptides from human MHC class I molecules alongside alanine and glycine point substitutions.
- HLA-E bound weakly to the mouse Qa-1-associated leader sequence peptide but bound nonamer signal sequence-derived peptides from human MHC class I molecules.
- Alanine and glycine substitutions mapped primary anchor residues to peptide positions 2 and 9, alongside secondary anchor residues at position 7 and potentially position 3.
Cite This Study
Braud et al. (1997) studied this question.