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8ES7

CryoEM structure of PN45545 TCR-CD3 complex

Summary for 8ES7
Entry DOI10.2210/pdb8es7/pdb
EMDB information28570 28571 28572 28573 28574
DescriptorT-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 Keywordstcr, membrane protein, cd3, immune system
Biological sourceHomo sapiens (human)
More
Total number of polymer chains8
Total formula weight196949.93
Authors
Saotome, K.,Franklin, M.C. (deposition date: 2022-10-13, release date: 2023-05-03, Last modification date: 2024-10-30)
Primary citationSaotome, 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: 37100770
DOI: 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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