4QRR
Crystal Structure of HLA B*3501-IPS in complex with a Delta-Beta TCR, clone 12 TCR
Summary for 4QRR
Entry DOI | 10.2210/pdb4qrr/pdb |
Related | 4QRP 4QRQ 4QRR 4QRS 4QRT |
Descriptor | HLA class I histocompatibility antigen, B-35 alpha chain, Beta-2-microglobulin, clone12 TCR beta chain, ... (6 entities in total) |
Functional Keywords | hla b*3501, human cmv, tcr, t cell, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 5 |
Total formula weight | 94921.44 |
Authors | Gras, S.,Chabrol, E.,Rossjohn, J. (deposition date: 2014-07-02, release date: 2014-12-10, Last modification date: 2024-11-27) |
Primary citation | Pellicci, D.G.,Uldrich, A.P.,Le Nours, J.,Ross, F.,Chabrol, E.,Eckle, S.B.,de Boer, R.,Lim, R.T.,McPherson, K.,Besra, G.,Howell, A.R.,Moretta, L.,McCluskey, J.,Heemskerk, M.H.,Gras, S.,Rossjohn, J.,Godfrey, D.I. The molecular bases of delta / alpha beta T cell-mediated antigen recognition. J.Exp.Med., 211:2599-2615, 2014 Cited by PubMed Abstract: αβ and γδ T cells are disparate T cell lineages that can respond to distinct antigens (Ags) via the use of the αβ and γδ T cell Ag receptors (TCRs), respectively. Here we characterize a population of human T cells, which we term δ/αβ T cells, expressing TCRs comprised of a TCR-δ variable gene (Vδ1) fused to joining α and constant α domains, paired with an array of TCR-β chains. We demonstrate that these cells, which represent ∼50% of all Vδ1(+) human T cells, can recognize peptide- and lipid-based Ags presented by human leukocyte antigen (HLA) and CD1d, respectively. Similar to type I natural killer T (NKT) cells, CD1d-lipid Ag-reactive δ/αβ T cells recognized α-galactosylceramide (α-GalCer); however, their fine specificity for other lipid Ags presented by CD1d, such as α-glucosylceramide, was distinct from type I NKT cells. Thus, δ/αβTCRs contribute new patterns of Ag specificity to the human immune system. Furthermore, we provide the molecular bases of how δ/αβTCRs bind to their targets, with the Vδ1-encoded region providing a major contribution to δ/αβTCR binding. Our findings highlight how components from αβ and γδTCR gene loci can recombine to confer Ag specificity, thus expanding our understanding of T cell biology and TCR diversity. PubMed: 25452463DOI: 10.1084/jem.20141764 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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