4Y16
Crystal structure of the mCD1d/NC-aGC/iNKTCR ternary complex
4Y16 の概要
| エントリーDOI | 10.2210/pdb4y16/pdb |
| 関連するPDBエントリー | 4Y2D 4Y4F 4Y4H 4Y4K |
| 分子名称 | Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, Chimeric TCR Valpha14/Jalpha18 chain (mouse variable domain, human constant domain), ... (9 entities in total) |
| 機能のキーワード | mhc-fold, ig-fold, glycolipid antigen presentation, t cell receptor, 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 | 96619.29 |
| 構造登録者 | |
| 主引用文献 | Birkholz, A.,Nemcovic, M.,Yu, E.D.,Girardi, E.,Wang, J.,Khurana, A.,Pauwels, N.,Farber, E.,Chitale, S.,Franck, R.W.,Tsuji, M.,Howell, A.,Van Calenbergh, S.,Kronenberg, M.,Zajonc, D.M. Lipid and Carbohydrate Modifications of alpha-Galactosylceramide Differently Influence Mouse and Human Type I Natural Killer T Cell Activation. J.Biol.Chem., 290:17206-17217, 2015 Cited by PubMed Abstract: The ability of different glycosphingolipids (GSLs) to activate type I natural killer T cells (NKT cells) has been known for 2 decades. The possible therapeutic use of these GSLs has been studied in many ways; however, studies are needed in which the efficacy of promising GSLs is compared under identical conditions. Here, we compare five unique GSLs structurally derived from α-galactosylceramide. We employed biophysical and biological assays, as well as x-ray crystallography to study the impact of the chemical modifications of the antigen on type I NKT cell activation. Although all glycolipids are bound by the T cell receptor of type I NKT cells in real time binding assays with high affinity, only a few activate type I NKT cells in in vivo or in vitro experiments. The differences in biological responses are likely a result of different pharmacokinetic properties of each lipid, which carry modifications at different parts of the molecule. Our results indicate a need to perform a variety of assays to ascertain the therapeutic potential of type I NKT cell GSL activators. PubMed: 26018083DOI: 10.1074/jbc.M115.654814 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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