6MRA
Diversity in the type II Natural Killer T cell receptor repertoire and antigen specificity leads to differing CD1d docking strategies
Summary for 6MRA
Entry DOI | 10.2210/pdb6mra/pdb |
Descriptor | TCR alpha chain, TCR beta-chain (3 entities in total) |
Functional Keywords | nkt cells, cd1d molecule, microbial lipid antigen, immune system |
Biological source | Mus musculus More |
Total number of polymer chains | 2 |
Total formula weight | 50056.43 |
Authors | Sundararaj, S.,Le Nours, J.,Praveena, T.,Rossjohn, J. (deposition date: 2018-10-12, release date: 2019-09-18, Last modification date: 2024-11-06) |
Primary citation | Almeida, C.F.,Sundararaj, S.,Le Nours, J.,Praveena, T.,Cao, B.,Burugupalli, S.,Smith, D.G.M.,Patel, O.,Brigl, M.,Pellicci, D.G.,Williams, S.J.,Uldrich, A.P.,Godfrey, D.I.,Rossjohn, J. Distinct CD1d docking strategies exhibited by diverse Type II NKT cell receptors. Nat Commun, 10:5242-5242, 2019 Cited by PubMed Abstract: Type I and type II natural killer T (NKT) cells are restricted to the lipid antigen-presenting molecule CD1d. While we have an understanding of the antigen reactivity and function of type I NKT cells, our knowledge of type II NKT cells in health and disease remains unclear. Here we describe a population of type II NKT cells that recognise and respond to the microbial antigen, α-glucuronosyl-diacylglycerol (α-GlcADAG) presented by CD1d, but not the prototypical type I NKT cell agonist, α-galactosylceramide. Surprisingly, the crystal structure of a type II NKT TCR-CD1d-α-GlcADAG complex reveals a CD1d F'-pocket-docking mode that contrasts sharply with the previously determined A'-roof positioning of a sulfatide-reactive type II NKT TCR. Our data also suggest that diverse type II NKT TCRs directed against distinct microbial or mammalian lipid antigens adopt multiple recognition strategies on CD1d, thereby maximising the potential for type II NKT cells to detect different lipid antigens. PubMed: 31748533DOI: 10.1038/s41467-019-12941-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report