1mhe
From Proteopedia
THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E
Overview
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.
About this Structure
1MHE is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E., O'Callaghan CA, Tormo J, Willcox BE, Braud VM, Jakobsen BK, Stuart DI, McMichael AJ, Bell JI, Jones EY, Mol Cell. 1998 Mar;1(4):531-41. PMID:9660937 Page seeded by OCA on Sat May 3 01:01:53 2008
Categories: Homo sapiens | Protein complex | Bell, J I. | Braud, V B. | Callaghan, C A.O. | Jakobsen, B K. | Jones, E Y. | Mcmichael, A J. | Stuart, D I. | Tormo, J. | Willcox, B E. | Beta 2 microglobulin | Class ib mhc | Hla | Hla e | Hla-e | Leader peptide | Major histocompatibility complex | Mhc | Non-classical mhc | Peptide
