1MHE

THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E

Summary for 1MHE

• Entry DOI: 10.2210/pdb1mhe/pdb
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN HLA-E, BETA-2-MICROGLOBULIN, PEPTIDE (VMAPRTVLL), ... (5 entities in total)
• Functional Keywords: hla-e, hla e, major histocompatibility complex, mhc, hla, beta 2 microglobulin, leader peptide, non-classical mhc, class ib mhc
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P13747; Secreted: P61769
• Total number of polymer chains: 6
• Total formula weight: 89251.04

Authors

O'Callaghan, C.A.,Tormo, J.,Willcox, B.E.,Braud, V.B.,Jakobsen, B.K.,Stuart, D.I.,Mcmichael, A.J.,Bell, J.I.,Jones, E.Y. (deposition date: 1998-08-24, release date: 1999-03-23, Last modification date: 2024-10-09)

Primary citation

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.
Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.
Mol.Cell, 1:531-541, 1998

PubMed 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.

PubMed: 9660937
DOI: 10.1016/S1097-2765(00)80053-2

Experimental method

X-RAY DIFFRACTION (2.85 Å)