4Z4V

Crystal structure of GII.10 P domain in complex with 19mM fucose

Summary for 4Z4V

• Entry DOI: 10.2210/pdb4z4v/pdb
• Descriptor: Capsid protein, NITRATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: fucose, norovirus, protruding domain, viral protein
• Biological source: Norovirus GII.10
• Total number of polymer chains: 2
• Total formula weight: 69736.03

Authors

Koromyslova, A.D.,Leuthold, M.M.,Hansman, G.S. (deposition date: 2015-04-02, release date: 2015-05-27, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)