3rug
Crystal structure of Valpha10-Vbeta8.1 NKT TCR in complex with CD1d-alphaglucosylceramide (C20:2)
Structural highlights
FunctionCD1D1_MOUSE Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.[1] [2] [3] Publication Abstract from PubMedType I natural killer T cells (NKT cells) are characterized by an invariant variable region 14-joining region 18 (V(alpha)14-J(alpha)18) T cell antigen receptor (TCR) alpha-chain and recognition of the glycolipid alpha-galactosylceramide (alpha-GalCer) restricted to the antigen-presenting molecule CD1d. Here we describe a population of alpha-GalCer-reactive NKT cells that expressed a canonical V(alpha)10-J(alpha)50 TCR alpha-chain, which showed a preference for alpha-glucosylceramide (alpha-GlcCer) and bacterial alpha-glucuronic acid-containing glycolipid antigens. Structurally, despite very limited TCRalpha sequence identity, the V(alpha)10 TCR-CD1d-alpha-GlcCer complex had a docking mode similar to that of type I TCR-CD1d-alpha-GalCer complexes, although differences at the antigen-binding interface accounted for the altered antigen specificity. Our findings provide new insight into the structural basis and evolution of glycolipid antigen recognition and have notable implications for the scope and immunological role of glycolipid-specific T cell responses. A semi-invariant V(alpha)10(+) T cell antigen receptor defines a population of natural killer T cells with distinct glycolipid antigen-recognition properties.,Uldrich AP, Patel O, Cameron G, Pellicci DG, Day EB, Sullivan LC, Kyparissoudis K, Kjer-Nielsen L, Vivian JP, Cao B, Brooks AG, Williams SJ, Illarionov P, Besra GS, Turner SJ, Porcelli SA, McCluskey J, Smyth MJ, Rossjohn J, Godfrey DI Nat Immunol. 2011 Jun 12;12(7):616-23. doi: 10.1038/ni.2051. PMID:21666690[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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