3AXL

Murine Valpha 10 Vbeta 8.1 T-cell receptor

3AXL の概要

• エントリーDOI: 10.2210/pdb3axl/pdb
• 分子名称: Valpha 10, Vbeta 8.1 (3 entities in total)
• 機能のキーワード: immunoglobulin fold, t-cell receptor, cd1d binding, 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: 97001.11

構造登録者

Patel, O.,Rossjohn, J. (登録日: 2011-04-11, 公開日: 2011-08-03, 最終更新日: 2024-10-09)

主引用文献

Uldrich, A.P.,Patel, O.,Cameron, G.,Pellicci, D.G.,Day, E.B.,Sullivan, L.C.,Kyparissoudis, K.,Kjer-Nielsen, L.,Vivian, J.P.,Cao, B.,Brooks, A.G.,Williams, S.J.,Illarionov, P.,Besra, G.S.,Turner, S.J.,Porcelli, S.A.,McCluskey, J.,Smyth, M.J.,Rossjohn, J.,Godfrey, D.I.
A semi-invariant V(alpha)10(+) T cell antigen receptor defines a population of natural killer T cells with distinct glycolipid antigen-recognition properties
Nat.Immunol., 12:616-623, 2011

PubMed Abstract: Type I natural killer T cells (NKT cells) are characterized by an invariant variable region 14-joining region 18 (V(α)14-J(α)18) T cell antigen receptor (TCR) α-chain and recognition of the glycolipid α-galactosylceramide (α-GalCer) restricted to the antigen-presenting molecule CD1d. Here we describe a population of α-GalCer-reactive NKT cells that expressed a canonical V(α)10-J(α)50 TCR α-chain, which showed a preference for α-glucosylceramide (α-GlcCer) and bacterial α-glucuronic acid-containing glycolipid antigens. Structurally, despite very limited TCRα sequence identity, the V(α)10 TCR-CD1d-α-GlcCer complex had a docking mode similar to that of type I TCR-CD1d-α-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.

PubMed: 21666690
DOI: 10.1038/ni.2051

実験手法

X-RAY DIFFRACTION (2.9 Å)