3ILP

Structure of mCD1d with bound glycolipid BbGL-2f from Borrelia burgdorferi

3ILP の概要

• エントリーDOI: 10.2210/pdb3ilp/pdb
• 関連するPDBエントリー: 1ZHN 2FIK 3ILQ
• 分子名称: T-cell surface glycoprotein CD1d1, Beta-2 microglobulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: antigen presentation. inkt cells, glycolipid, host defense, cell membrane, disulfide bond, endosome, glycoprotein, immune response, immunoglobulin domain, innate immunity, lysosome, membrane, transmembrane, mhc i, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45774.81

構造登録者

Zajonc, D.M. (登録日: 2009-08-07, 公開日: 2010-01-26, 最終更新日: 2024-10-16)

主引用文献

Wang, J.,Li, Y.,Kinjo, Y.,Mac, T.T.,Gibson, D.,Painter, G.F.,Kronenberg, M.,Zajonc, D.M.
Lipid binding orientation within CD1d affects recognition of Borrelia burgorferi antigens by NKT cells.
Proc.Natl.Acad.Sci.USA, 107:1535-1540, 2010

PubMed Abstract: Invariant natural killer T cells (iNKT cells) respond to CD1d-presented glycolipids from Borrelia burgdorferi, the causative agent of Lyme disease. Although mouse and human iNKT cells respond to different antigens based on subtle differences in their fatty acids, the mechanism by which fatty acid structure determines antigenic potency is not well understood. Here we show that the mouse and human CD1d present glycolipids having different fatty acids, based in part upon a difference at a single amino acid position that is involved in positioning the sugar epitope. CD1d also can bind nonantigenic lipids, however, but unexpectedly, mouse CD1d orients the two aliphatic chains of a nonantigenic lipid rotated 180 degrees, causing a dramatic repositioning of the exposed sugar. Therefore, our data reveal the biochemical basis for the high degree of antigenic specificity of iNKT cells for certain fatty acids, and they suggest how microbes could alter fatty acid biosynthesis as an immune evasion mechanism.

PubMed: 20080535
DOI: 10.1073/pnas.0909479107

実験手法

X-RAY DIFFRACTION (1.85 Å)