 |
PDBsum entry 2obs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
2obs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis for the recognition of blood group trisaccharides by norovirus.
|
|
|
Authors
|
|
S.Cao,
Z.Lou,
M.Tan,
Y.Chen,
Y.Liu,
Z.Zhang,
X.C.Zhang,
X.Jiang,
X.Li,
Z.Rao.
|
|
|
Ref.
|
|
J Virol, 2007,
81,
5949-5957.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
