Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6CQN

Crystal structure of F5 TCR -DR11-RQ13 peptide complex

Summary for 6CQN
Entry DOI10.2210/pdb6cqn/pdb
DescriptorHLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-11 beta chain, Peptide from Capsid protein p24, ... (10 entities in total)
Functional Keywordstcr, immune receptor, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains5
Total formula weight96740.56
Authors
Farenc, C.,Gras, S.,Rossjohn, J. (deposition date: 2018-03-15, release date: 2018-06-06, Last modification date: 2024-11-06)
Primary citationGalperin, 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: 29884618
DOI: 10.1126/sciimmunol.aat0687
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

227344

건을2024-11-13부터공개중

PDB statisticsPDBj update infoContact PDBjnumon