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Structure paper

TitleStructures of human γδ T cell receptor-CD3 complex.
Journal, issue, pagesNature, Year 2024
Publish dateApr 24, 2024
AuthorsWeizhi Xin / Bangdong Huang / Ximin Chi / Yuehua Liu / Mengjiao Xu / Yuanyuan Zhang / Xu Li / Qiang Su / Qiang Zhou /
PubMed AbstractGamma delta (γδ) T cells, a unique T cell subgroup, are crucial in various immune responses and immunopathology. The γδ T cell receptor (TCR), generated by γδ T cells, recognizes a diverse ...Gamma delta (γδ) T cells, a unique T cell subgroup, are crucial in various immune responses and immunopathology. The γδ T cell receptor (TCR), generated by γδ T cells, recognizes a diverse range of antigens independently of the major histocompatibility complex. The γδ TCR associates with CD3 subunits, initiating T cell activation and holding great potential in immunotherapy. Here, we report the structures of two prototypical human Vγ9Vδ2 and Vγ5Vδ1 TCR-CD3 complexes, unveiling two distinct assembly mechanisms that depend on Vγ usage. The Vγ9Vδ2 TCR-CD3 complex is monomeric, with considerable conformational flexibility in the TCRγ/TCRδ extracellular domain (ECD) and connecting peptides (CPs). The length of CPs regulates the ligand association and T cell activation. Additionally, a cholesterol-like molecule wedges into the transmembrane region, exerting an inhibitory role in TCR signaling. The Vγ5Vδ1 TCR-CD3 complex displays a dimeric architecture, where two protomers nestle back-to-back via their Vγ5 domains of TCR ECDs. Our biochemical and biophysical assays further corroborate the dimeric structure. Importantly, the dimeric form of the Vγ5Vδ1 TCR is essential for T cell activation. These findings reveal organizing principles of the γδ TCR-CD3 complex, providing insights into the γδ TCR unique properties and facilitating immunotherapeutic interventions.
External linksNature / PubMed:38657677
MethodsEM (single particle)
Resolution3.0 - 9.5 Å
Structure data

36147

8jbv

EMDB-36147, PDB-8jbv:
Extracellular domain of gamma delta TCR
Method: EM (single particle) / Resolution: 3.02 Å

36149

8jc0

EMDB-36149, PDB-8jc0:
V gamma9 V delta2 TCR and CD3 complex in LMNG
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-36152: Vgamma5 Vdelta1 TCR complex (MPDI/TMDI)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-36153: Vgamma5 Vdelta1 TCR complex (MPDII/TMDII)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-36155: Vgamma5 Vdelta1 TCR complex (MPD/TMD)
Method: EM (single particle) / Resolution: 5.7 Å

36156

8jcb

EMDB-36156, PDB-8jcb:
Vgamma5 Vdelta1 T cell receptor complex
Method: EM (single particle) / Resolution: 9.5 Å

37904

8wxe

EMDB-37904, PDB-8wxe:
Vgamma5Vdelta1 EH TCR-CD3 complex
Method: EM (single particle) / Resolution: 4.0 Å

37914

8wy0

EMDB-37914, PDB-8wy0:
T cell receptor delta 2 gamma 9 with F283A, F290A, and F291A
Method: EM (single particle) / Resolution: 3.8 Å

37929

8wyi

EMDB-37929, PDB-8wyi:
T cell receptor delta 2 gamma 9 with TCRD TM domain chimera of TRAC
Method: EM (single particle) / Resolution: 3.9 Å

39128

8yc0

EMDB-39128, PDB-8yc0:
T cell receptor V delta2 V gamma9 in GDN
Method: EM (single particle) / Resolution: 4.12 Å

EMDB-39359: T cell receptor V delta2 V gamma9 in GDN (DeepEMhancer)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-39361: Vgamma5 Vdelta1 TCR complex (MPDI/TMDI, DeepEMhancer)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-39362: Vgamma5 Vdelta1 TCR complex (MPDII/TMDII, DeepEMhancer)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-39363: V gamma9 V delta2 TCR and CD3 complex in LMNG (DeepEMhancer)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-39367: Vgamma5 Vdelta1 TCR-CD3 complex (EH mutant, DeepEMhancer)
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-39368: Extracellular domain of Vgamma5 Vdelta1 TCR (DeepEMhancer)
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL / Cholesterol

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Receptor / immunity / immune

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