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Human histocompatibility leukocyte antigen E (HLA-E) and mouse major histocompatibility complex (MHC) class Ib antigen, Qa-1, share the same substitutions at two normally conserved positions 143 and 147, which are likely to affect binding of the C terminus of peptides. Qa-1 is able to bind a peptide derived from the leader sequence of H-2 D and H-2 L molecules. We developed a peptide binding assay in vitro to compare the binding specificity of HLA-E with the mouse MHC class Ib molecule Qa-1. We demonstrate that HLA-E binds, although poorly, the peptide which binds to Qa-1 and that it also binds nonamer signal sequence-derived peptides from human MHC class I molecules. Using alanine and glycine substitutions, we could define primary anchor residues at positions 2 and 9 and secondary anchor residues at position 7 and possibly 3.

Original publication

DOI

10.1002/eji.1830270517

Type

Journal article

Journal

Eur J Immunol

Publication Date

05/1997

Volume

27

Pages

1164 - 1169

Keywords

Amino Acid Sequence, Animals, Cell Line, Transformed, HLA Antigens, Histocompatibility Antigens Class I, Humans, Isoelectric Focusing, L Cells (Cell Line), Mice, Oligopeptides, Protein Binding, Protein Conformation, Protein Sorting Signals