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6CQQ

Crystal structure of F24 TCR -DR15-RQ13 peptide complex

Summary for 6CQQ
Entry DOI10.2210/pdb6cqq/pdb
DescriptorHLA class II histocompatibility antigen, DR alpha chain, HLA-DRB1 protein, Peptide from Capsid protein p24, ... (10 entities in total)
Functional Keywordstcr, immune receptor, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains10
Total formula weight192362.05
Authors
Farenc, C.,Gras, S.,Rossjohn, J. (deposition date: 2018-03-16, release date: 2018-06-06, Last modification date: 2024-10-16)
Primary 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 (2.8 Å)
Structure validation

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건을2024-11-06부터공개중

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