8ES7
CryoEM structure of PN45545 TCR-CD3 complex
Summary for 8ES7
Entry DOI | 10.2210/pdb8es7/pdb |
EMDB information | 28570 28571 28572 28573 28574 |
Descriptor | T-cell surface glycoprotein CD3 zeta chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, T-cell surface glycoprotein CD3 delta chain, ... (10 entities in total) |
Functional Keywords | tcr, membrane protein, cd3, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 8 |
Total formula weight | 196949.93 |
Authors | Saotome, K.,Franklin, M.C. (deposition date: 2022-10-13, release date: 2023-05-03, Last modification date: 2024-10-30) |
Primary citation | Saotome, K.,Dudgeon, D.,Colotti, K.,Moore, M.J.,Jones, J.,Zhou, Y.,Rafique, A.,Yancopoulos, G.D.,Murphy, A.J.,Lin, J.C.,Olson, W.C.,Franklin, M.C. Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEM. Nat Commun, 14:2401-2401, 2023 Cited by PubMed Abstract: The recognition of antigenic peptide-MHC (pMHC) molecules by T-cell receptors (TCR) initiates the T-cell mediated immune response. Structural characterization is key for understanding the specificity of TCR-pMHC interactions and informing the development of therapeutics. Despite the rapid rise of single particle cryoelectron microscopy (cryoEM), x-ray crystallography has remained the preferred method for structure determination of TCR-pMHC complexes. Here, we report cryoEM structures of two distinct full-length α/β TCR-CD3 complexes bound to their pMHC ligand, the cancer-testis antigen HLA-A2/MAGEA4 (230-239). We also determined cryoEM structures of pMHCs containing MAGEA4 (230-239) peptide and the closely related MAGEA8 (232-241) peptide in the absence of TCR, which provided a structural explanation for the MAGEA4 preference displayed by the TCRs. These findings provide insights into the TCR recognition of a clinically relevant cancer antigen and demonstrate the utility of cryoEM for high-resolution structural analysis of TCR-pMHC interactions. PubMed: 37100770DOI: 10.1038/s41467-023-37532-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.04 Å) |
Structure validation
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