1Z2K

NMR structure of the D1 domain of the Natural Killer Cell Receptor, 2B4

1Z2K の概要

• エントリーDOI: 10.2210/pdb1z2k/pdb
• 分子名称: Natural killer cell receptor 2B4 (1 entity in total)
• 機能のキーワード: immunoglobulin motif, beta sandwich, v-domain, natural killer cell receptor, immune system
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): Q07763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12210.55

構造登録者

Ames, J.B.,Vyas, V.,Lusin, J.D.,Mariuzza, R. (登録日: 2005-03-08, 公開日: 2005-05-03, 最終更新日: 2024-10-30)

主引用文献

Ames, J.B.,Vyas, V.,Lusin, J.D.,Mariuzza, R.
NMR Structure of the Natural Killer Cell Receptor 2B4: Implications for Ligand Recognition
Biochemistry, 44:6416-6423, 2005

PubMed Abstract: 2B4, a transmembrane receptor expressed primarily on natural killer (NK) cells and on a subset of CD8(+) T cells, plays an important role in activating NK-mediated cytotoxicity through its interaction with CD48 on target cells. We report here the atomic-resolution structure of the ligand-binding (D1) domain of 2B4 in solution determined by nuclear magnetic resonance (NMR) spectroscopy. The overall main chain structure resembles an immunoglobulin variable (V) domain fold, very similar to that seen previously for domain 1 of CD2 and CD4. The structure contains nine beta-strands assembled into two beta-sheets conventionally labeled DEB and AGFCC'C' '. The six-stranded sheet (AGFCC'C' ') contains structural features that may have implications for ligand recognition and receptor function. A noncanonical disulfide bridge between Cys2 and Cys99 stabilizes a long and parallel beta-structure between strand A (residues 3-12) and strand G (residues 100-108). A beta-bulge at residues Glu45 and Ile46 places a bend in the middle of strand C' that orients two conserved and adjacent hydrophobic residues (Ile46 and Leu47) inside the beta-sandwich as seen in other V domains. Finally, the FG-loop (implicated in ligand recognition in the CD2-CD58 complex) is dynamically disordered in 2B4 in the absence of a ligand. We propose that ligand binding to 2B4 might stabilize the structure of the FG-loop in the ligand complex.

PubMed: 15850375
DOI: 10.1021/bi050139s

実験手法

SOLUTION NMR