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3SKM

Crystal structure of the HLA-B8FLRGRAYVL, mutant G8V of the FLR peptide

Summary for 3SKM
Entry DOI10.2210/pdb3skm/pdb
Related1KGC 1M05 1MI5 3FFC 3SJV 3SKN 3SKO
DescriptorHLA class I histocompatibility antigen, B-8 alpha chain, Beta-2-microglobulin, Epstein-Barr nuclear antigen 3, ... (4 entities in total)
Functional Keywordst cell receptor, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P30460
Secreted: P61769
Host nucleus matrix: Q3KST2
Total number of polymer chains3
Total formula weight44903.66
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 citationGras, 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: 22140258
DOI: 10.4049/jimmunol.1102686
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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