Summary for 6QZC
| Entry DOI | 10.2210/pdb6qzc/pdb |
| Related | 6EH6 6QZA 6QZD 6R0E |
| Descriptor | HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-1 beta chain, M1-208-222-QAR-Peptide, ... (8 entities in total) |
| Functional Keywords | hla-dr1, cd4, t-cell, influenza, matrix, conserved, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 45512.12 |
| Authors | Greenshields-Watson, A.,Rizkallah, P.J. (deposition date: 2019-03-11, release date: 2020-07-15, Last modification date: 2024-10-16) |
| Primary citation | Greenshields-Watson, A.,Attaf, M.,MacLachlan, B.J.,Whalley, T.,Rius, C.,Wall, A.,Lloyd, A.,Hughes, H.,Strange, K.E.,Mason, G.H.,Schauenburg, A.J.,Hulin-Curtis, S.L.,Geary, J.,Chen, Y.,Lauder, S.N.,Smart, K.,Vijaykrishna, D.,Grau, M.L.,Shugay, M.,Andrews, R.,Dolton, G.,Rizkallah, P.J.,Gallimore, A.M.,Sewell, A.K.,Godkin, A.J.,Cole, D.K. CD4+T Cells Recognize Conserved Influenza A Epitopes through Shared Patterns of V-Gene Usage and Complementary Biochemical Features. Cell Rep, 32:107885-107885, 2020 Cited by PubMed Abstract: T cell recognition of peptides presented by human leukocyte antigens (HLAs) is mediated by the highly variable T cell receptor (TCR). Despite this built-in TCR variability, individuals can mount immune responses against viral epitopes by using identical or highly related TCRs expressed on CD8 T cells. Characterization of these TCRs has extended our understanding of the molecular mechanisms that govern the recognition of peptide-HLA. However, few examples exist for CD4 T cells. Here, we investigate CD4 T cell responses to the internal proteins of the influenza A virus that correlate with protective immunity. We identify five internal epitopes that are commonly recognized by CD4 T cells in five HLA-DR1 subjects and show conservation across viral strains and zoonotic reservoirs. TCR repertoire analysis demonstrates several shared gene usage biases underpinned by complementary biochemical features evident in a structural comparison. These epitopes are attractive targets for vaccination and other T cell therapies. PubMed: 32668259DOI: 10.1016/j.celrep.2020.107885 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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