6CQQ
Crystal structure of F24 TCR -DR15-RQ13 peptide complex
Summary for 6CQQ
Entry DOI | 10.2210/pdb6cqq/pdb |
Descriptor | HLA class II histocompatibility antigen, DR alpha chain, HLA-DRB1 protein, Peptide from Capsid protein p24, ... (10 entities in total) |
Functional Keywords | tcr, immune receptor, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 10 |
Total formula weight | 192362.05 |
Authors | Farenc, C.,Gras, S.,Rossjohn, J. (deposition date: 2018-03-16, release date: 2018-06-06, Last modification date: 2024-10-16) |
Primary citation | 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 Cited by 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: 29884618DOI: 10.1126/sciimmunol.aat0687 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report