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6CPH

Crystal structure of the F24 TCR

Summary for 6CPH
Entry DOI10.2210/pdb6cph/pdb
DescriptorTCR alpha chain, TCR beta chain, SULFATE ION, ... (5 entities in total)
Functional Keywordstcr, immune receptor, immune system
Biological sourceHomo sapiens
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Total number of polymer chains2
Total formula weight51195.73
Authors
Farenc, C.,Gras, S.,Rossjohn, J. (deposition date: 2018-03-13, release date: 2018-06-06, Last modification date: 2024-10-23)
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 (1.7 Å)
Structure validation

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