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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | 1C5H TCR bound to R-phycoerythrin | |||||||||
![]() | R-Phycoerythrin | |||||||||
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![]() | T-cell / gamma delta TCR / phycoerythrin / direct / IMMUNE SYSTEM | |||||||||
Function / homology | Phycobilisome, alpha/beta subunit / Phycobilisome, alpha/beta subunit superfamily / Phycobilisome protein / phycobilisome / chloroplast thylakoid membrane / photosynthesis / Globin-like superfamily / R-phycoerythrin class I beta subunit / R-phycoerythrin class I alpha subunit![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 1.68 Å | |||||||||
![]() | Rashleigh L / Venugopal H / Rossjohn J / Gully BS | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Antibody-like recognition of a γδ T cell receptor toward a foreign antigen. Authors: Liam Rashleigh / Hariprasad Venugopal / Michael T Rice / Sachith D Gunasinghe / Chhon Ling Sok / Nicholas A Gherardin / Catarina F Almeida / Ildiko Van Rhijn / D Branch Moody / Dale I ...Authors: Liam Rashleigh / Hariprasad Venugopal / Michael T Rice / Sachith D Gunasinghe / Chhon Ling Sok / Nicholas A Gherardin / Catarina F Almeida / Ildiko Van Rhijn / D Branch Moody / Dale I Godfrey / Jamie Rossjohn / Benjamin S Gully / ![]() ![]() ![]() Abstract: The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells ...The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells can directly bind proteinaceous antigens. A known γδ T cell and B cell model antigen is phycoerythrin (PE), a light harvesting protein from rhodophytes and cyanobacteria. Here we probed human γδTCR reactivity to PE, in which a Vδ1Vγ5 TCR bound directly to induce proximal signaling and cellular activation. We determined the cryoelectron microscopy (cryo-EM) structure of the γδTCR-phycoerythrin immune complex. We then determined the cryo-EM structures of an antibody fragment and an αβTCR bound to PE. This revealed convergent use of apical aromatic residues to mediate contacts with a common PE epitope. Comparative analyses of the γδTCR revealed multiple antibody-like characteristics, including an enrichment of apical aromatic residues. Our findings reveal further distinct facets of antigen recognition by the γδTCR. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 90.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.7 KB 18.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.4 KB | Display | ![]() |
Images | ![]() | 109.3 KB | ||
Masks | ![]() | 178 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() ![]() | 167.7 MB 165.1 MB 165.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 903.5 KB | Display | ![]() |
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Full document | ![]() | 903.1 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 27 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9o61MC ![]() 9mgbC ![]() 9mkoC ![]() 9o60C ![]() 9o62C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | R-Phycoerythrin | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.82 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: sharpened map
File | emd_70156_additional_1.map | ||||||||||||
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Annotation | sharpened map | ||||||||||||
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-Half map: Half Map A
File | emd_70156_half_map_1.map | ||||||||||||
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Annotation | Half Map A | ||||||||||||
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-Half map: Half Map B
File | emd_70156_half_map_2.map | ||||||||||||
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Annotation | Half Map B | ||||||||||||
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Density Histograms |
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Sample components
-Entire : R-phycoerythrin
Entire | Name: R-phycoerythrin |
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Components |
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-Supramolecule #1: R-phycoerythrin
Supramolecule | Name: R-phycoerythrin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: R-phycoerythrin class I alpha subunit
Macromolecule | Name: R-phycoerythrin class I alpha subunit / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 17.707906 KDa |
Sequence | String: MKSVITTTIS AADAAGRFPS SSDLESVQGN IQRAASRLEA AEKLAGNHEA VVKEAGDACF AKYPYLKNPG EAGDSQEKIN KCYRDIDHY MRLINYSLVV GGTGPLDEWG IAGAREVYRA LNLPGSSYIA AFVFTRDRLC VPRDMSAQAA VEFSGALDYV I NSLC UniProtKB: R-phycoerythrin class I alpha subunit |
-Macromolecule #2: R-phycoerythrin class I beta subunit
Macromolecule | Name: R-phycoerythrin class I beta subunit / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 18.33685 KDa |
Sequence | String: MLDAFSRVVV NSDSKAAYVS GSDLQALKTF IADGNKRLDA VNSIVSNASC IVSDAVSGMI CENPGLIAPG GNCYTNRRMA ACLRDGEII LRYTSYALLA GDSSVLEDRC LNGLKETYIA LGVPTNSTAR AVSIMKSSAV AFISNTAPQR KMATAAGDCS A LSSEVASY CDKVSAAI UniProtKB: R-phycoerythrin class I beta subunit |
-Macromolecule #3: PHYCOERYTHROBILIN
Macromolecule | Name: PHYCOERYTHROBILIN / type: ligand / ID: 3 / Number of copies: 24 / Formula: PEB |
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Molecular weight | Theoretical: 588.694 Da |
Chemical component information | ![]() ChemComp-PEB: |
-Macromolecule #4: PHYCOUROBILIN
Macromolecule | Name: PHYCOUROBILIN / type: ligand / ID: 4 / Number of copies: 6 / Formula: PUB |
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Molecular weight | Theoretical: 590.71 Da |
Chemical component information | ![]() ChemComp-CYB: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |