3SKO
Crystal structure of the HLA-B8-A66-FLR, mutant A66 of the HLA B8
3SKO の概要
| エントリーDOI | 10.2210/pdb3sko/pdb |
| 関連するPDBエントリー | 1KGC 1M05 1MI5 3FFC 3SJV 3SKM 3SKN |
| 分子名称 | HLA class I histocompatibility antigen, B-8 alpha chain, Beta-2-microglobulin, Epstein-Barr nuclear antigen 3, ... (5 entities in total) |
| 機能のキーワード | t cell receptor, immune system, antigen presentation |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Membrane; Single-pass type I membrane protein: P30460 Secreted: P61769 Host nucleus matrix: Q3KST2 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 44929.57 |
| 構造登録者 | Gras, S.,Wilmann, P.G.,Zhenjun, C.,Hanim, H.,Yu Chih, L.,Kjer-Nielsen, L.,Purcell, A.W.,Burrows, S.R.,Mccluskey, J.,Rossjohn, J. (登録日: 2011-06-22, 公開日: 2012-02-29, 最終更新日: 2024-11-27) |
| 主引用文献 | Gras, S.,Wilmann, P.G.,Chen, Z.,Halim, H.,Liu, Y.C.,Kjer-Nielsen, L.,Purcell, A.W.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. A structural basis for varied alpha-beta TCR usage against an immunodominant EBV antigen restricted to a HLA-B8 molecule. J.Immunol., 188:311-321, 2012 Cited by PubMed Abstract: EBV is a ubiquitous and persistent human pathogen, kept in check by the cytotoxic T cell response. In this study, we investigated how three TCRs, which differ in their T cell immunodominance hierarchies and gene usage, interact with the same EBV determinant (FLRGRAYGL), bound to the same Ag-presenting molecule, HLA-B8. We found that the three TCRs exhibit differing fine specificities for the viral Ag. Further, via structural and biophysical approaches, we demonstrated that the viral Ag provides the greatest energetic contribution to the TCR-peptide-HLA interaction, while focusing on a few adjacent HLA-based interactions to further tune fine-specificity requirements. Thus, the TCR engages the peptide-HLA with the viral Ag as the main glue, such that neighboring TCR-MHC interactions are recruited as a supportive adhesive. Collectively, we provide a portrait of how the host's adaptive immune response differentially engages a common viral Ag. PubMed: 22140258DOI: 10.4049/jimmunol.1102686 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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