2obt
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Crystal Structures of P Domain of Norovirus VA387 in Complex with Blood Group Trisaccharides type B
OverviewOverview
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 location and receptor binding, mode of HBGA carbohydrates on the viral capsids, a recombinant P protein, of a GII-4 strain norovirus, VA387, was co-crystallized with synthetic, types A- or B-trisaccharides. Based on complex crystal structures at 2.0-A, resolution, we demonstrated that the receptor-binding site lies at the, outmost end of the P domain and forms an extensive hydrogen-bonding, network with the saccharide ligand. The A- and B-trisaccharides share, similar binding modes, and the common fucose ring played 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.
About this StructureAbout this Structure
2OBT is a Single protein structure of sequence from Nairovirus. Full crystallographic information is available from OCA.
ReferenceReference
Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus., Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z, J Virol. 2007 Mar 28;. PMID:17392366
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