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...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
1998
|
| _version_ | 1797085290574118912 |
|---|---|
| author | O'Callaghan, C Tormo, J Willcox, B Braud, V Jakobsen, B Stuart, D Mcmichael, A Bell, J Jones, E |
| author_facet | O'Callaghan, C Tormo, J Willcox, B Braud, V Jakobsen, B Stuart, D Mcmichael, A Bell, J Jones, E |
| author_sort | O'Callaghan, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T02:06:49Z |
| format | Journal article |
| id | oxford-uuid:9f49657c-c833-4b27-86b1-fd84e35993f8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:06:49Z |
| publishDate | 1998 |
| record_format | dspace |
| spelling | oxford-uuid:9f49657c-c833-4b27-86b1-fd84e35993f82022-03-27T00:56:26ZStructural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9f49657c-c833-4b27-86b1-fd84e35993f8EnglishSymplectic Elements at Oxford1998O'Callaghan, CTormo, JWillcox, BBraud, VJakobsen, BStuart, DMcmichael, ABell, JJones, EThe 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. |
| spellingShingle | O'Callaghan, C Tormo, J Willcox, B Braud, V Jakobsen, B Stuart, D Mcmichael, A Bell, J Jones, E Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title | Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title_full | Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title_fullStr | Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title_full_unstemmed | Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title_short | Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. |
| title_sort | structural features impose tight peptide binding specificity in the nonclassical mhc molecule hla e |
| work_keys_str_mv | AT ocallaghanc structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT tormoj structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT willcoxb structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT braudv structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT jakobsenb structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT stuartd structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT mcmichaela structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT bellj structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae AT jonese structuralfeaturesimposetightpeptidebindingspecificityinthenonclassicalmhcmoleculehlae |