5HYJ
1E6 TCR in Complex with HLA-A02 carrying AQWGPDPAAA
Summary for 5HYJ
Entry DOI | 10.2210/pdb5hyj/pdb |
Related | 5C07 5C08 5C09 5C0A 5C0B 5C0C 5C0D 5C0E 5C0F 5C0G 5C0H 5C0I 5C0J |
Descriptor | HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, ALA-GLN-TRP-GLY-PRO-ASP-PRO-ALA-ALA-ALA, ... (6 entities in total) |
Functional Keywords | immuno, hla-a02, 1e6-tcr, cross-reactivity, immune system |
Biological source | Homo sapiens (Human) More |
Cellular location | Membrane; Single-pass type I membrane protein: P01892 Secreted : P61769 |
Total number of polymer chains | 10 |
Total formula weight | 189064.48 |
Authors | Rizkallah, P.J.,Bulek, A.M.,Cole, D.K.,Sewell, A.K. (deposition date: 2016-02-01, release date: 2016-05-04, Last modification date: 2024-01-10) |
Primary citation | Stadinski, B.D.,Obst, R.,Huseby, E.S. A "hotspot" for autoimmune T cells in type 1 diabetes. J.Clin.Invest., 126:2040-2042, 2016 Cited by PubMed Abstract: The ability of a single T cell antigen receptor (TCR) to cross-react with multiple antigens allows the finite number of T cells within an organism to respond to the compendium of pathogen challenges faced during a lifetime. Effective immune surveillance, however, comes at a price. TCR cross-reactivity can allow molecular mimics to spuriously activate autoimmune T cells; it also underlies T cell rejection of organ transplants and drives graft-versus-host disease. In this issue of the JCI, Cole and colleagues provide insight into how an insulin-reactive T cell cross-reacts with pathogen-derived antigens by focusing on a limited portion of the peptides to provide a hotspot for binding. These findings dovetail with recent studies of alloreactive and autoimmune TCRs and suggest that the biochemical principles that govern conventional protein-protein interactions may allow the specificity and cross-reactivity profiles of T cells to be predicted. PubMed: 27183386DOI: 10.1172/JCI88165 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.06 Å) |
Structure validation
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