3SJV
Crystal structure of the RL42 TCR in complex with HLA-B8-FLR
Summary for 3SJV
| Entry DOI | 10.2210/pdb3sjv/pdb |
| Related | 1KGC 1M05 1MI5 3FFC 3SKM 3SKN 3SKO |
| Descriptor | HLA class I histocompatibility antigen, B-8 alpha chain, Beta-2-microglobulin, Epstein-Barr nuclear antigen 3, ... (5 entities in total) |
| Functional Keywords | t cell, immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 20 |
| Total formula weight | 380389.85 |
| Authors | Gras, S.,Wilmann, P.G.,Zhenjun, C.,Hanim, H.,Yu Chih, L.,Kjer-Nielsen, L.,Purcell, A.W.,Burrows, S.R.,Mccluskey, J.,Rossjohn, J. (deposition date: 2011-06-22, release date: 2012-02-29, Last modification date: 2024-11-20) |
| Primary citation | Gras, S.,Wilmann, P.G.,Chen, Z.,Halim, H.,Liu, Y.C.,Kjer-Nielsen, L.,Purcell, A.W.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. A structural basis for varied alpha-beta TCR usage against an immunodominant EBV antigen restricted to a HLA-B8 molecule. J.Immunol., 188:311-321, 2012 Cited by PubMed Abstract: EBV is a ubiquitous and persistent human pathogen, kept in check by the cytotoxic T cell response. In this study, we investigated how three TCRs, which differ in their T cell immunodominance hierarchies and gene usage, interact with the same EBV determinant (FLRGRAYGL), bound to the same Ag-presenting molecule, HLA-B8. We found that the three TCRs exhibit differing fine specificities for the viral Ag. Further, via structural and biophysical approaches, we demonstrated that the viral Ag provides the greatest energetic contribution to the TCR-peptide-HLA interaction, while focusing on a few adjacent HLA-based interactions to further tune fine-specificity requirements. Thus, the TCR engages the peptide-HLA with the viral Ag as the main glue, such that neighboring TCR-MHC interactions are recruited as a supportive adhesive. Collectively, we provide a portrait of how the host's adaptive immune response differentially engages a common viral Ag. PubMed: 22140258DOI: 10.4049/jimmunol.1102686 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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