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3SKO

Crystal structure of the HLA-B8-A66-FLR, mutant A66 of the HLA B8

3SKO の概要
エントリーDOI10.2210/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: 22140258
DOI: 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)
構造検証レポート
Validation report summary of 3sko
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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