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PDBsum entry 1k3v
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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 structure of porcine parvovirus: comparison with related viruses.
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Authors
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A.A.Simpson,
B.Hébert,
G.M.Sullivan,
C.R.Parrish,
Z.Zádori,
P.Tijssen,
M.G.Rossmann.
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Ref.
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J Mol Biol, 2002,
315,
1189-1198.
[DOI no: ]
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PubMed id
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Abstract
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The structure of baculovirus-expressed porcine parvovirus (PPV) capsids was
solved using X-ray crystallography and was found to be similar to the related
canine parvovirus (CPV) and minute virus of mice (MVM). The PPV capsid protein
has 57 % and 49 % amino acid sequence identity with CPV and MVM, respectively,
but the degree of conservation of surface-exposed residues is lower than
average. Consequently, most of the structural differences are on the surface and
are the probable cause of the known variability in antigenicity and host range.
The NADL-2 and Kresse strains of PPV have distinct tissue tropisms and
pathogenicity, which are mediated by one or more of the amino acid residues 381,
386, and 436. These residues are on or near the surface of the virus capsid,
where they are likely to be associated with virus-cell interactions.
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Figure 3.
Figure 3. Surface view of residues (yellow) that control
tissue tropism. Residue 436 is near the 3-fold spike and
residues 378 and 383 are near the edge of the 2-fold dimple,
with 383 being nearer the surface. (a) van der Waals surface
representation of these residues with the rest of the capsid
shown as a C^a backbone trace. (b) Suface representation of all
atoms in the capsid, with one subunit shown in orange.
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Figure 5.
Figure 5. Conservation of surface features of PPV relative
to FPV and MVM. (a) PPV compared to FPV; (b) PPV compared to
MVM, with red being the most conserved and blue being the most
variable. Left stereo figures show surface views and right mono
figures show central cross-sections. Symmetry axes are shown in
white.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2002,
315,
1189-1198)
copyright 2002.
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