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PDBsum entry 1c8h
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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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Host range and variability of calcium binding by surface loops in the capsids of canine and feline parvoviruses.
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Authors
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A.A.Simpson,
V.Chandrasekar,
B.Hébert,
G.M.Sullivan,
M.G.Rossmann,
C.R.Parrish.
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Ref.
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J Mol Biol, 2000,
300,
597-610.
[DOI no: ]
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PubMed id
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Abstract
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Canine parvovirus (CPV) emerged in 1978 as a host range variant of feline
panleukopenia virus (FPV). This change of host was mediated by the mutation of
five residues on the surface of the capsid. CPV and FPV enter cells by
endocytosis and can be taken up by many non-permissive cell lines, showing that
their host range and tissue specificity are largely determined by events
occurring after cell entry.We have determined the structures of a variety of
strains of CPV and FPV at various pH values and in the presence or absence of
Ca(2+). The largest structural difference was found to occur in a flexible
surface loop, consisting of residues 359 to 375 of the capsid protein. This loop
binds a divalent calcium ion in FPV and is adjacent to a double Ca(2+)-binding
site, both in CPV and FPV. Residues within the loop and those associated with
the double Ca(2+)-binding site were found to be essential for virus infectivity.
The residues involved in the double Ca(2+)-binding site are conserved only in
FPV and CPV.Our results show that the loop conformation and the associated
Ca(2+)-binding are influenced by the Ca(2+) concentration, as well as pH. These
changes are correlated with the ability of the virus to hemagglutinate
erythrocytes. The co-localization of hemagglutinating activity and host range
determinants on the virus surface implies that these properties may be
functionally linked. We speculate that the flexible loop and surrounding regions
are involved in binding an as yet unidentified host molecule and that this
interaction influences host range.
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Figure 4.
Figure 4. Histogram showing distribution of inter-Ca^2+
distances in structures in the PDB. The broken line shows the
distance between sites 2 and 3 in CPV and FPV.
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Figure 5.
Figure 5. Stereodiagrams showing the environment of the
double Ca^2+-binding sites 1, 2, and 3 in relation to the
flexible loop. (a) FPV, pH 6.2 (ID7). (b) FPV, pH 7.5 (ID3). (c)
CPV, pH 7.5 (ID1). (d) CPV A300D, pH 7.5 (ID4). (e) FPV, pH 6.2
EDTA (ID10). These figures were prepared using the programs
XTALVIEW [McRee 1993] and Raster3D [Merritt and Bacon 1997].
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2000,
300,
597-610)
copyright 2000.
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Secondary reference #1
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Title
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Structure determination of feline panleukopenia virus empty particles.
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Authors
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M.Agbandje,
R.Mckenna,
M.G.Rossmann,
M.L.Strassheim,
C.R.Parrish.
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Ref.
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Proteins, 1993,
16,
155-171.
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PubMed id
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Secondary reference #2
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Title
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Structural refinement of the DNA-Containing capsid of canine parvovirus using rsref, A resolution-Dependent stereochemically restrained real-Space refinement method.
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Authors
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M.S.Chapman,
M.G.Rossmann.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1996,
52,
129-142.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Steps in he refinement of
DNAcontaining canine parvo
virus. For comparative purposes,
the R factors were all calculated
using ,1000 eflections selected at
random beween 5 and 3.25,~,
resolutions, for which F > 5¢r r.
Table 10 shows R factors calcu
lated to higher resolution and with
out additional
F/cr F
selection.
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Figure 3.
Fig. 3. Fit of the model to eectron density. The upper stereoram shows
residues 214217 of the starting mdel (thin lines), model RS1
(medium) and moel RS2 (thick lines) superimposed upon the
eectrondensity ap of Tsao et al. (1991). The starting model was
refied against this map to yield model RSI, which after some
manual rebuilding was further refined to RS2. The lower stereogram
illustrates the later sages of refiement, showing RS2 (dashed lines)
and RS4 (solid lines) superimposed n the final map. The final map
was based on phases calcuated from RS2 and then refned by 60fold
smmetry averaging. This figure was prepared using the program O
(Jones et al., 1991).
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #3
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Title
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Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range.
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Authors
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A.L.Llamas-Saiz,
M.Agbandje-Mckenna,
J.S.Parker,
A.T.Wahid,
C.R.Parrish,
M.G.Rossmann.
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Ref.
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Virology, 1996,
225,
65-71.
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PubMed id
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Secondary reference #4
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Title
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The three-Dimensional structure of canine parvovirus and its functional implications.
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Authors
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J.Tsao,
M.S.Chapman,
M.Agbandje,
W.Keller,
K.Smith,
H.Wu,
M.Luo,
T.J.Smith,
M.G.Rossmann,
R.W.Compans.
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Ref.
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Science, 1991,
251,
1456-1464.
[DOI no: ]
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PubMed id
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