5HZB

Crystal structure of GII.10 P domain in complex with 2-fucosyllactose (2'FL)

Summary for 5HZB

Entry DOI	10.2210/pdb5hzb/pdb
Descriptor	Capsid protein, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywords	norovirus capsid, p domain, hmo, human milk, 2-fucosyllactose, virus, viral protein
Biological source	Norovirus GII.10
Total number of polymer chains	2
Total formula weight	69750.03
Authors	Hansman, G.S.,Koromyslova, A.D.,Singh, B.K.S. (deposition date: 2016-02-02, release date: 2016-03-02, Last modification date: 2024-01-10)
Primary citation	Weichert, S.,Koromyslova, A.,Singh, B.K.,Hansman, S.,Jennewein, S.,Schroten, H.,Hansman, G.S. Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides. J.Virol., 90:4843-4848, 2016 Cited by PubMed Abstract: Histo-blood group antigens (HBGAs) are important binding factors for norovirus infections. We show that two human milk oligosaccharides, 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL), could block norovirus from binding to surrogate HBGA samples. We found that 2'FL and 3FL bound at the equivalent HBGA pockets on the norovirus capsid using X-ray crystallography. Our data revealed that 2'FL and 3FL structurally mimic HBGAs. These results suggest that 2'FL and 3FL might act as naturally occurring decoys in humans. PubMed: 26889023 DOI: 10.1128/JVI.03223-15 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.553 Å)

Structure validation