1mhe
From Proteopedia
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THE HUMAN NON-CLASSICAL MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE HLA-E
Contents |
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.
Disease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this Structure
1MHE is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. 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 Mon Nov 12 18:11:16 2007
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. | SO4 | Beta 2 microglobulin | Class ib mhc | Hla | Hla e | Hla-e | Leader peptide | Major histocompatibility complex | Mhc | Non-classical mhc | Peptide
