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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

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

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.[1]

References

  1. Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. O'Callaghan, C.A., Tormo, J., Willcox, B.E., Braud, V.M., Jakobsen, B.K., Stuart, D.I., McMichael, A.J., Bell, J.I., Jones, E.Y. Mol. Cell (1998) [Pubmed]
 
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