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6MSS

Diversity in the type II Natural Killer T cell receptor repertoire and antigen specificity leads to differing CD1d docking strategies

Summary for 6MSS
Entry DOI10.2210/pdb6mss/pdb
DescriptorA11B8.2 NKT TCR alpha-chain, A11B8.2 NKT TCR beta-chain, Antigen-presenting glycoprotein CD1d1, ... (8 entities in total)
Functional Keywordsnkt cells, cd1d molecule, microbial lipid antigen, immune system
Biological sourceMus musculus (Mouse)
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Total number of polymer chains4
Total formula weight98046.75
Authors
Sundararaj, S.,Le Nours, J.,Praveena, T.,Rossjohn, J. (deposition date: 2018-10-18, release date: 2019-10-02, Last modification date: 2024-11-06)
Primary citationAlmeida, 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: 31748533
DOI: 10.1038/s41467-019-12941-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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