3SKN

Crystal structure of the RL42 TCR unliganded

3SKN の概要

• エントリーDOI: 10.2210/pdb3skn/pdb
• 関連するPDBエントリー: 1KGC 1M05 1MI5 3FFC 3SJV 3SKM 3SKO
• 分子名称: RL42 T cell receptor, alpha chain, RL42 T cell receptor, beta chain (2 entities in total)
• 機能のキーワード: t cell receptor, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 200595.22

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: 2024-11-06)

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

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

実験手法

X-RAY DIFFRACTION (2.9 Å)