2Q7Y
Structure of the endogenous iNKT cell ligand iGb3 bound to mCD1d
2Q7Y の概要
| エントリーDOI | 10.2210/pdb2q7y/pdb |
| 関連するPDBエントリー | 1Z5L 2AKR 2FIK 2GAZ |
| 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, ... (8 entities in total) |
| 機能のキーワード | antigen presenting molecule, mhc fold, nkt cells, immune system |
| 由来する生物種 | Mus musculus (house mouse) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 93346.35 |
| 構造登録者 | |
| 主引用文献 | Zajonc, D.M.,Savage, P.B.,Bendelac, A.,Wilson, I.A.,Teyton, L. Crystal Structures of Mouse CD1d-iGb3 Complex and its Cognate Valpha14 T Cell Receptor Suggest a Model for Dual Recognition of Foreign and Self Glycolipids. J.Mol.Biol., 377:1104-1116, 2008 Cited by PubMed Abstract: The semi-invariant Valpha14Jalpha18 T cell receptor (TCR) is expressed by regulatory NKT cells and has the unique ability to recognize chemically diverse ligands presented by CD1d. The crystal structure of CD1d complexed to a natural, endogenous ligand, isoglobotrihexosylceramide (iGb3), illustrates the extent of this diversity when compared to the binding of potent, exogenous ligands, such as alpha-galactosylceramide (alpha-GalCer). A single mode of recognition for these two classes of ligands would then appear problematic for a single T cell receptor. However, the Valpha14 TCR adopts two different conformations in the crystal where, in one configuration, the presence of a larger cavity between the two CDR3 regions could accommodate iGb3 and, in the other, a smaller cavity fits alpha-GalCer more snugly. Alternatively, the extended iGb3 headgroup could be "squashed" upon docking of the TCR and accommodated between the CD1 and TCR surfaces. Thus, the same TCR may adopt alternative modes of recognition for these foreign and self-ligands for NKT cell activation. PubMed: 18295796DOI: 10.1016/j.jmb.2008.01.061 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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