2OBS

Crystal Structures of P Domain of Norovirus VA387 in Complex with Blood Group Trisaccharides type A

Summary for 2OBS

• Entry DOI: 10.2210/pdb2obs/pdb
• Related: 2OBR 2OBT
• Descriptor: Capsid protein, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-gulopyranose (3 entities in total)
• Functional Keywords: crystal structures, p domain, norovirus va387, blood group trisaccharides type a, viral protein
• Biological source: Norovirus
• Total number of polymer chains: 1
• Total formula weight: 36511.70

Authors

Cao, S.,Li, X.,Rao, Z. (deposition date: 2006-12-20, release date: 2007-04-24, Last modification date: 2023-10-25)

Primary citation

Cao, S.,Lou, Z.,Tan, M.,Chen, Y.,Liu, Y.,Zhang, Z.,Zhang, X.C.,Jiang, X.,Li, X.,Rao, Z.
Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus
J.Virol., 81:5949-5957, 2007

PubMed Abstract: Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.

PubMed: 17392366
DOI: 10.1128/JVI.00219-07

Experimental method

X-RAY DIFFRACTION (2 Å)