6CQQ

Crystal structure of F24 TCR -DR15-RQ13 peptide complex

6CQQ の概要

• エントリーDOI: 10.2210/pdb6cqq/pdb
• 分子名称: HLA class II histocompatibility antigen, DR alpha chain, HLA-DRB1 protein, Peptide from Capsid protein p24, ... (10 entities in total)
• 機能のキーワード: tcr, immune 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: 10
• 化学式量合計: 192362.05

構造登録者

Farenc, C.,Gras, S.,Rossjohn, J. (登録日: 2018-03-16, 公開日: 2018-06-06, 最終更新日: 2024-10-16)

主引用文献

Galperin, M.,Farenc, C.,Mukhopadhyay, M.,Jayasinghe, D.,Decroos, A.,Benati, D.,Tan, L.L.,Ciacchi, L.,Reid, H.H.,Rossjohn, J.,Chakrabarti, L.A.,Gras, S.
CD4+T cell-mediated HLA class II cross-restriction in HIV controllers.
Sci Immunol, 3:-, 2018

PubMed Abstract: Rare individuals, termed HIV controllers, spontaneously control HIV infection by mounting efficient T cell responses against the virus. Protective CD4 T cell responses from HIV controllers involve high-affinity public T cell receptors (TCRs) recognizing an immunodominant capsid epitope (Gag293) presented by a remarkably broad array of human leukocyte antigen (HLA) class II molecules. Here, we determine the structures of a prototypical public TCR bound to HLA-DR1, HLA-DR11, and HLA-DR15 molecules presenting the Gag293 epitope. TCR recognition was driven by contacts with the Gag293 epitope, a feature that underpinned the extensive HLA cross-restriction. These high-affinity TCRs promoted mature immunological synapse formation and cytotoxic capacity in both CD4 and CD8 T cells. The public TCRs suppressed HIV replication in multiple genetic backgrounds ex vivo, emphasizing the functional advantage conferred by broad HLA class II cross-restriction.

PubMed: 29884618
DOI: 10.1126/sciimmunol.aat0687

実験手法

X-RAY DIFFRACTION (2.8 Å)