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Yorodumi- EMDB-70155: Local refinement of 1C5H TCR bound to R-phycoerythrin (gamma chai... -
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Basic information
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| Title | Local refinement of 1C5H TCR bound to R-phycoerythrin (gamma chain dimer) | |||||||||
Map data | Local refinement of 1C5H TCR bound to R-phycoerythrin (gamma chain dimer) | |||||||||
Sample |
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Keywords | T-cell / gamma delta TCR / phycoerythrin / direct / IMMUNE SYSTEM | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.63 Å | |||||||||
Authors | Rashleigh L / Venugopal H / Rossjohn J / Gully BS | |||||||||
| Funding support | Australia, 1 items
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Citation | Journal: Structure / Year: 2025Title: 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. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_70155.map.gz | 89.4 MB | EMDB map data format | |
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| Header (meta data) | emd-70155-v30.xml emd-70155.xml | 19.2 KB 19.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_70155_fsc.xml | 12.5 KB | Display | FSC data file |
| Images | emd_70155.png | 63.6 KB | ||
| Masks | emd_70155_msk_1.map | 178 MB | Mask map | |
| Filedesc metadata | emd-70155.cif.gz | 5.9 KB | ||
| Others | emd_70155_additional_1.map.gz emd_70155_half_map_1.map.gz emd_70155_half_map_2.map.gz | 168.1 MB 165.4 MB 165.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-70155 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-70155 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9o60MC ![]() 9mgbC ![]() 9mkoC ![]() 9o61C ![]() 9o62C M: atomic model generated by this map C: citing same article ( |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_70155.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Local refinement of 1C5H TCR bound to R-phycoerythrin (gamma chain dimer) | ||||||||||||||||||||||||||||||||||||
| 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
| File | emd_70155_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: sharpened map.
| File | emd_70155_additional_1.map | ||||||||||||
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| Annotation | sharpened map. | ||||||||||||
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| Density Histograms |
-Half map: Half Map B
| File | emd_70155_half_map_1.map | ||||||||||||
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| Annotation | Half Map B | ||||||||||||
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| Density Histograms |
-Half map: Half Map A
| File | emd_70155_half_map_2.map | ||||||||||||
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| Annotation | Half Map A | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : 1C5H TCR
| Entire | Name: 1C5H TCR |
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| Components |
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-Supramolecule #1: 1C5H TCR
| Supramolecule | Name: 1C5H TCR / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: 1C5H TCR gamma chain
| Macromolecule | Name: 1C5H TCR gamma chain / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 27.014568 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: SSNLEGGTKS VTRPTRSSAE ITCDLTVINA FYIHWYLHQE GKAPQRLLYY DVSNSKDVLE SGLSPGKYYT HTPRRWSWIL ILRNLIEND SGVYYCATWD RPSKLFGSGT TLVVTDKQLD ADVSPKPTIF LPSIAETKLQ KAGTYLCLLE KFFPDVIKIH W QEKKSNTI ...String: SSNLEGGTKS VTRPTRSSAE ITCDLTVINA FYIHWYLHQE GKAPQRLLYY DVSNSKDVLE SGLSPGKYYT HTPRRWSWIL ILRNLIEND SGVYYCATWD RPSKLFGSGT TLVVTDKQLD ADVSPKPTIF LPSIAETKLQ KAGTYLCLLE KFFPDVIKIH W QEKKSNTI LGSQEGNTMK TNDTYMKFSW LTVPEESLDK EHRCIVRHEN NKNGVDQEII FPPIKTDVIT MDPKDNASG |
-Macromolecule #2: 1C5H TCR delta chain
| Macromolecule | Name: 1C5H TCR delta chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 26.886508 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: AQKVTQAQSS VSMPVRKAVT LNCLYETSWW SYYIFWYKQL PSKEMIFLIR QGSDEQNAKS GRYSVNFKKA AKSVALTISA LQLEDSAKY FCALGAPHTY WGISTDLSSW DTRQMFFGTG IKLFVEPRSQ PHTKPSVFVM KNGTNVACLV KEFYPKDIRI N LVSSKKIT ...String: AQKVTQAQSS VSMPVRKAVT LNCLYETSWW SYYIFWYKQL PSKEMIFLIR QGSDEQNAKS GRYSVNFKKA AKSVALTISA LQLEDSAKY FCALGAPHTY WGISTDLSSW DTRQMFFGTG IKLFVEPRSQ PHTKPSVFVM KNGTNVACLV KEFYPKDIRI N LVSSKKIT EFDPAIVISP SGKYNAVKLG KYEDSNSVTC SVQHDNKTVH STDFEVKTDS TDHVKPKETE NTKQPSKSAS G |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | 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: FIELD EMISSION GUN |
| 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 |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Australia, 1 items
Citation











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Processing
FIELD EMISSION GUN

