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- EMDB-28572: CryoEM structure of PN45428 TCR-CD3 in complex with HLA-A2 MAGEA4 -
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Open data
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Basic information
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Title | CryoEM structure of PN45428 TCR-CD3 in complex with HLA-A2 MAGEA4 | |||||||||
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![]() | TCR / ![]() ![]() ![]() | |||||||||
Function / homology | ![]() regulation of lymphocyte apoptotic process / gamma-delta T cell receptor complex / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Saotome K / Franklin MC | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEM. Authors: Kei Saotome / Drew Dudgeon / Kiersten Colotti / Michael J Moore / Jennifer Jones / Yi Zhou / Ashique Rafique / George D Yancopoulos / Andrew J Murphy / John C Lin / William C Olson / Matthew C Franklin / ![]() 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 ...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. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 270.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.4 KB 24.4 KB | Display Display | ![]() |
Images | ![]() | 74.2 KB | ||
Filedesc metadata | ![]() | 7.2 KB | ||
Others | ![]() ![]() | 261.4 MB 261.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8es9MC ![]() 8es7C ![]() 8es8C ![]() 8esaC ![]() 8esbC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.85 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
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Density Histograms |
-Half map: #2
File | emd_28572_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : PN45428 TCR-CD3 complex bound to HLA-A2 MAGEA4 (230-239) in the p...
+Supramolecule #1: PN45428 TCR-CD3 complex bound to HLA-A2 MAGEA4 (230-239) in the p...
+Macromolecule #1: PN45428 TCR alpha chain
+Macromolecule #2: PN45428 TCR beta chain
+Macromolecule #3: T-cell surface glycoprotein CD3 zeta chain
+Macromolecule #4: T-cell surface glycoprotein CD3 delta chain
+Macromolecule #5: T-cell surface glycoprotein CD3 epsilon chain
+Macromolecule #6: T-cell surface glycoprotein CD3 gamma chain
+Macromolecule #7: MHC class I antigen
+Macromolecule #8: Beta-2-microglobulin
+Macromolecule #9: Melanoma-associated antigen 4
+Macromolecule #12: 2-acetamido-2-deoxy-beta-D-glucopyranose
+Macromolecule #13: CHOLESTEROL HEMISUCCINATE
-Experimental details
-Structure determination
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.25 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 107308 |