8wxe | pdb_00008wxe

Vgamma5Vdelta1 EH TCR-CD3 complex

spinqualitylabelsall models 8wxe, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8wxe is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4Å Ligands: CLR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease CD3Z_HUMAN Defects in CD247 are the cause of immunodeficiency due to defect in CD3-zeta (CD3ZID) [MIM:610163. An immunological deficiency characterized by T-cells impaired immune response to alloantigens, tetanus toxoid and mitogens. Function CD3Z_HUMAN Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering. Publication Abstract from PubMed Gamma delta (gammadelta) T cells, a unique T cell subgroup, are crucial in various immune responses and immunopathology(1-3). The gammadelta T cell receptor (TCR), generated by gammadelta T cells, recognizes a diverse range of antigens independently of the major histocompatibility complex(2). The gammadelta TCR associates with CD3 subunits, initiating T cell activation and holding great potential in immunotherapy(4). Here, we report the structures of two prototypical human Vgamma9Vdelta2 and Vgamma5Vdelta1 TCR-CD3 complexes(5,6), unveiling two distinct assembly mechanisms that depend on Vgamma usage. The Vgamma9Vdelta2 TCR-CD3 complex is monomeric, with considerable conformational flexibility in the TCRgamma/TCRdelta 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 Vgamma5Vdelta1 TCR-CD3 complex displays a dimeric architecture, where two protomers nestle back-to-back via their Vgamma5 domains of TCR ECDs. Our biochemical and biophysical assays further corroborate the dimeric structure. Importantly, the dimeric form of the Vgamma5Vdelta1 TCR is essential for T cell activation. These findings reveal organizing principles of the gammadelta TCR-CD3 complex, providing insights into the gammadelta TCR unique properties and facilitating immunotherapeutic interventions. Structures of human gammadelta T cell receptor-CD3 complex.,Xin W, Huang B, Chi X, Liu Y, Xu M, Zhang Y, Li X, Su Q, Zhou Q Nature. 2024 Apr 24. doi: 10.1038/s41586-024-07439-4. PMID:38657677 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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