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PDBsum entry 1kqr
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Viral protein
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PDB id
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1kqr
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The rhesus rotavirus vp4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.
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Authors
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P.R.Dormitzer,
Z.Y.Sun,
G.Wagner,
S.C.Harrison.
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Ref.
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EMBO J, 2002,
21,
885-897.
[DOI no: ]
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PubMed id
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Abstract
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Cell attachment and membrane penetration are functions of the rotavirus outer
capsid spike protein, VP4. An activating tryptic cleavage of VP4 produces the
N-terminal fragment, VP8*, which is the viral hemagglutinin and an important
target of neutralizing antibodies. We have determined, by X-ray crystallography,
the atomic structure of the VP8* core bound to sialic acid and, by NMR
spectroscopy, the structure of the unliganded VP8* core. The domain has the
beta-sandwich fold of the galectins, a family of sugar binding proteins. The
surface corresponding to the galectin carbohydrate binding site is blocked, and
rotavirus VP8* instead binds sialic acid in a shallow groove between its two
beta-sheets. There appears to be a small induced fit on binding. The residues
that contact sialic acid are conserved in sialic acid-dependent rotavirus
strains. Neutralization escape mutations are widely distributed over the VP8*
surface and cluster in four epitopes. From the fit of the VP8* core into the
virion spikes, we propose that VP4 arose from the insertion of a host
carbohydrate binding domain into a viral membrane interaction protein.
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Figure 1.
Figure 1 The rotavirus triple-layered virion. VP4 and VP7 make
up the outer capsid, which constitutes the entry apparatus. The
RNA, VP2 and VP6 are the major structural components of the
double-layered particle, which is the transcriptionally active
core. The line drawing is based on an electron
cryomicroscopy-based reconstruction (Yeager et al., 1990).
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Figure 6.
Figure 6 Surface representations of the rotavirus VP8^* core,
colored according to the variability between the rotavirus
strains listed in Table III. Blue represents the most conserved
surfaces and red represents the most variable surfaces. Labeled
amino acids indicate neutralization escape mutations (Table IV).
Labels colored by epitope: 8-1, green; 8-2, blue; 8-3, yellow;
8-4, pink; and not assigned, black. (A) As viewed along arrow 3
of Figure 7. (B) As viewed along arrow 1 and in panel B of
Figure 7. (C) As viewed along arrow 2 and in panel C of Figure
7. (A) and (C) are rotated 90° in either direction around
the horizontal axis relative to (B), as indicated by arrows on
the figure.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2002,
21,
885-897)
copyright 2002.
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Secondary reference #1
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Title
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Proteolysis of monomeric recombinant rotavirus vp4 yields an oligomeric vp5 Core.
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Authors
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P.R.Dormitzer,
H.B.Greenberg,
S.C.Harrison.
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Ref.
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J Virol, 2001,
75,
7339-7350.
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PubMed id
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