4P2O
Crystal structure of the 2B4 TCR in complex with 2A/I-Ek
Summary for 4P2O
Entry DOI | 10.2210/pdb4p2o/pdb |
Related | 4P2Q 4P2R |
Descriptor | H-2 class II histocompatibility antigen, E-K alpha chain, MHC class II E-beta-k, 2B4 T-cell receptor alpha chain, ... (8 entities in total) |
Functional Keywords | t cell receptor, immune system, peptide-mhc, complex |
Biological source | Mus musculus (Mouse) More |
Total number of polymer chains | 5 |
Total formula weight | 106936.81 |
Authors | Birnbaum, M.E.,Ozkan, E.,Garcia, K.C. (deposition date: 2014-03-04, release date: 2014-05-21, Last modification date: 2024-10-09) |
Primary citation | Birnbaum, M.E.,Mendoza, J.L.,Sethi, D.K.,Dong, S.,Glanville, J.,Dobbins, J.,Ozkan, E.,Davis, M.M.,Wucherpfennig, K.W.,Garcia, K.C. Deconstructing the Peptide-MHC Specificity of T Cell Recognition. Cell, 157:1073-1087, 2014 Cited by PubMed Abstract: In order to survey a universe of major histocompatibility complex (MHC)-presented peptide antigens whose numbers greatly exceed the diversity of the T cell repertoire, T cell receptors (TCRs) are thought to be cross-reactive. However, the nature and extent of TCR cross-reactivity has not been conclusively measured experimentally. We developed a system to identify MHC-presented peptide ligands by combining TCR selection of highly diverse yeast-displayed peptide-MHC libraries with deep sequencing. Although we identified hundreds of peptides reactive with each of five different mouse and human TCRs, the selected peptides possessed TCR recognition motifs that bore a close resemblance to their known antigens. This structural conservation of the TCR interaction surface allowed us to exploit deep-sequencing information to computationally identify activating microbial and self-ligands for human autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here enables effective surveillance of diverse self and foreign antigens without necessitating degenerate recognition of nonhomologous peptides. PubMed: 24855945DOI: 10.1016/j.cell.2014.03.047 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.603 Å) |
Structure validation
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