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

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… (More)

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Cite this paper

@article{OCallaghan1998StructuralFI, title={Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.}, author={Christopher A. O'Callaghan and Jos{\'e} Tormo and Benjamin E Willcox and V{\'e}ronique M Braud and Bent K. Jakobsen and David I Stuart and Andrew J McMichael and John I. Bell and E Yvonne Jones}, journal={Molecular cell}, year={1998}, volume={1 4}, pages={531-41} }