4Z4R

Crystal structure of GII.10 P domain in complex with 300mM fucose

4Z4R の概要

• エントリーDOI: 10.2210/pdb4z4r/pdb
• 分子名称: Capsid protein, 1,2-ETHANEDIOL, beta-L-fucopyranose, ... (4 entities in total)
• 機能のキーワード: fucose, norovirus, protruding domain, viral protein
• 由来する生物種: Norovirus GII.10
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69980.28

構造登録者

Koromyslova, A.D.,Leuthold, M.M.,Hansman, G.S. (登録日: 2015-04-02, 公開日: 2015-05-27, 最終更新日: 2024-01-10)

主引用文献

Koromyslova, A.D.,Leuthold, M.M.,Bowler, M.W.,Hansman, G.S.
The sweet quartet: Binding of fucose to the norovirus capsid.
Virology, 483:203-208, 2015

PubMed Abstract: Human noroviruses bind histo-blood group antigens (HBGAs) and this interaction is thought to be important for an infection. We identified two additional fucose-binding pockets (termed fucose-3/4 sites) on a genogroup II human (GII.10) norovirus-protruding (P) dimer using X-ray crystallography. Fucose-3/4 sites were located between two previously determined HBGA binding pockets (termed fucose-1/2 sites). We found that four fucose molecules were capable of binding altogether at fucose-1/2/3/4 sites on the P dimer, though the fucose molecules bound in a dose-dependent and step-wise manner. We also showed that HBGA B-trisaccharide molecules bound in a similar way at the fucose-1/2 sites. Interestingly, we discovered that the monomers of the P dimer were asymmetrical in an unliganded state and when a single B-trisaccharide molecule bound, but were symmetrical when two B-trisaccharide molecules bound. We postulate that the symmetrical dimers might favor HBGA binding interactions at fucose-1/2 sites.

PubMed: 25980740
DOI: 10.1016/j.virol.2015.04.006

実験手法

X-RAY DIFFRACTION (1.801 Å)