5KSA

Bel602-DQ8.5-glia-gamma1 complex

5KSA の概要

• エントリーDOI: 10.2210/pdb5ksa/pdb
• 関連するPDBエントリー: 5KS9 5KSB
• 分子名称: HLA class II histocompatibility antigen, DQ alpha 1 chain, HLA class II histocompatibility antigen, DQ beta 1 chain, Bel602 alpha TRAV20*01, ... (8 entities in total)
• 機能のキーワード: celiac disease t cell receptor peptide mhc complex, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 99386.08

構造登録者

Petersen, J.,Rossjohn, J.,Reid, H.H. (登録日: 2016-07-08, 公開日: 2016-09-21, 最終更新日: 2024-11-06)

主引用文献

Petersen, J.,Kooy-Winkelaar, Y.,Loh, K.L.,Tran, M.,van Bergen, J.,Koning, F.,Rossjohn, J.,Reid, H.H.
Diverse T Cell Receptor Gene Usage in HLA-DQ8-Associated Celiac Disease Converges into a Consensus Binding Solution.
Structure, 24:1643-1657, 2016

PubMed Abstract: In HLA-DQ8-associated celiac disease, TRAV26-2-TRBV9 and TRAV8-3-TRBV6 T cells recognize the immunodominant DQ8-glia-α1 epitope, whereupon a non-germline-encoded arginine residue played a key role in binding HLA-DQ8-glia-α1. Whether distinct T cell receptor (TCR) recognition modes exist for gliadin epitopes remains unclear. TCR repertoire analysis revealed populations of HLA-DQ8-glia-α1 and HLA-DQ8.5-glia-γ1 restricted TRAV20-TRBV9 T cells that did not possess a non-germline-encoded arginine residue. The crystal structures of a TRAV20-TRBV9 TCR-HLA-DQ8-glia-α1 complex and two TRAV20-TRBV9 TCR-HLA-DQ8.5-glia-γ1 complexes were determined. This revealed that the differential specificity toward DQ8-glia-α1 and DQ8.5-glia-γ1 was governed by CDR3β-loop-mediated interactions. Surprisingly, a germline-encoded arginine residue within the CDR1α loop of the TRAV20 TCR substituted for the role of the non-germline-encoded arginine in the TRAV26-2-TRBV9 and TRAV8-3-TRBV6 TCRs. Thus, in celiac disease, the responding TCR repertoire is driven by a common mechanism that selects for structural elements within the TCR that have convergent binding solutions in HLA-DQ8-gliadin recognition.

PubMed: 27568928
DOI: 10.1016/j.str.2016.07.010

実験手法

X-RAY DIFFRACTION (2 Å)