3SDC
Crystal structure of autoreactive-Valpha14-Vbeta6 NKT TCR in complex with CD1d-globotrihexosylceramide
3SDC の概要
エントリーDOI | 10.2210/pdb3sdc/pdb |
関連するPDBエントリー | 3SCM 3SDA 3SDD 3SDX |
分子名称 | Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, NKT TCR Valpha14 chain, ... (8 entities in total) |
機能のキーワード | cd1d, autoimmunity, self-recognition, nkt, immune system |
由来する生物種 | Mus musculus (mouse) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 98768.86 |
構造登録者 | |
主引用文献 | Pellicci, D.G.,Clarke, A.J.,Patel, O.,Mallevaey, T.,Beddoe, T.,Le Nours, J.,Uldrich, A.P.,McCluskey, J.,Besra, G.S.,Porcelli, S.A.,Gapin, L.,Godfrey, D.I.,Rossjohn, J. Recognition of beta-linked self glycolipids mediated by natural killer T cell antigen receptors Nat.Immunol., 12:827-833, 2011 Cited by PubMed Abstract: The most potent foreign antigens for natural killer T cells (NKT cells) are α-linked glycolipids, whereas NKT cell self-reactivity involves weaker recognition of structurally distinct β-linked glycolipid antigens. Here we provide the mechanism for the autoreactivity of T cell antigen receptors (TCRs) on NKT cells to the mono- and tri-glycosylated β-linked agonists β-galactosylceramide (β-GalCer) and isoglobotrihexosylceramide (iGb3), respectively. In binding these disparate antigens, the NKT cell TCRs docked onto CD1d similarly, achieving this by flattening the conformation of the β-linked ligands regardless of the size of the glycosyl head group. Unexpectedly, the antigenicity of iGb3 was attributable to its terminal sugar group making compensatory interactions with CD1d. Thus, the NKT cell TCR molds the β-linked self ligands to resemble the conformation of foreign α-linked ligands, which shows that induced-fit molecular mimicry can underpin the self-reactivity of NKT cell TCRs to β-linked antigens. PubMed: 21804559DOI: 10.1038/ni.2076 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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