6U3M

DQ2-P.fluor-alpha1a

6U3M の概要

• エントリーDOI: 10.2210/pdb6u3m/pdb
• 分子名称: HLA class II histocompatibility antigen, DQ alpha 1 chain, MHC class II HLA-DQ-beta-1, Alpha1a peptide, ... (8 entities in total)
• 機能のキーワード: immune complex, celiac disease, gliadin epitope, tcr cross-reactivity, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 96288.95

構造登録者

Petersen, J.,Rossjohn, J. (登録日: 2019-08-22, 公開日: 2019-12-18, 最終更新日: 2024-10-23)

主引用文献

Petersen, J.,Ciacchi, L.,Tran, M.T.,Loh, K.L.,Kooy-Winkelaar, Y.,Croft, N.P.,Hardy, M.Y.,Chen, Z.,McCluskey, J.,Anderson, R.P.,Purcell, A.W.,Tye-Din, J.A.,Koning, F.,Reid, H.H.,Rossjohn, J.
T cell receptor cross-reactivity between gliadin and bacterial peptides in celiac disease.
Nat.Struct.Mol.Biol., 27:49-61, 2020

PubMed Abstract: The human leukocyte antigen (HLA) locus is strongly associated with T cell-mediated autoimmune disorders. HLA-DQ2.5-mediated celiac disease (CeD) is triggered by the ingestion of gluten, although the relative roles of genetic and environmental risk factors in CeD is unclear. Here we identify microbially derived mimics of gliadin epitopes and a parental bacterial protein that is naturally processed by antigen-presenting cells and activated gliadin reactive HLA-DQ2.5-restricted T cells derived from CeD patients. Crystal structures of T cell receptors in complex with HLA-DQ2.5 bound to two distinct bacterial peptides demonstrate that molecular mimicry underpins cross-reactivity toward the gliadin epitopes. Accordingly, gliadin reactive T cells involved in CeD pathogenesis cross-react with ubiquitous bacterial peptides, thereby suggesting microbial exposure as a potential environmental factor in CeD.

PubMed: 31873306
DOI: 10.1038/s41594-019-0353-4

実験手法

X-RAY DIFFRACTION (1.9 Å)