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243 a.a.*
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278 a.a.*
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254 a.a.*
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238 a.a.*
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* Residue conservation analysis
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* C-alpha coords only
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PDB id:
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Virus/receptor
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Title:
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Structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy
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Structure:
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Decay-accelerating factor. Chain: r. Fragment: four scr domains 1 to 4. Engineered: yes. Coat protein vp1. Chain: 1. Engineered: yes. Coat protein vp2. Chain: 2.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Human echovirus 7. Organism_taxid: 46018. Expressed in: homo sapiens. Expression_system_taxid: 9606.
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Authors:
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Y.He,F.Lin,P.R.Chipman,C.M.Bator,T.S.Baker,M.Shoham,R.J.Kuhn, M.E.Medof,M.G.Rossmann
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Key ref:
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Y.He
et al.
(2002).
Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex.
Proc Natl Acad Sci U S A,
99,
10325-10329.
PubMed id:
DOI:
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Date:
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17-Jun-02
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Release date:
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28-Aug-02
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Headers
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References
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P08174
(DAF_HUMAN) -
Complement decay-accelerating factor from Homo sapiens
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Seq:
Struc:
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381 a.a.
243 a.a.
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Q914E0
(Q914E0_9ENTO) -
Genome polyprotein from Echovirus E7
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Seq:
Struc:
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2194 a.a.
278 a.a.
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Enzyme class 2:
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Chains 1, 2, 3:
E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Enzyme class 3:
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Chains 1, 2, 3:
E.C.3.4.22.28
- picornain 3C.
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Reaction:
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Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
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Enzyme class 4:
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Chains 1, 2, 3:
E.C.3.4.22.29
- picornain 2A.
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Reaction:
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Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
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Enzyme class 5:
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Chains 1, 2, 3:
E.C.3.6.1.15
- nucleoside-triphosphate phosphatase.
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Reaction:
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a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
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ribonucleoside 5'-triphosphate
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+
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H2O
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=
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ribonucleoside 5'-diphosphate
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+
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phosphate
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+
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H(+)
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Enzyme class 6:
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Chain R:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
99:10325-10329
(2002)
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PubMed id:
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Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex.
|
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Y.He,
F.Lin,
P.R.Chipman,
C.M.Bator,
T.S.Baker,
M.Shoham,
R.J.Kuhn,
M.E.Medof,
M.G.Rossmann.
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ABSTRACT
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Echoviruses are enteroviruses that belong to Picornaviridae. Many echoviruses
use decay-accelerating factor (DAF) as their cellular receptor. DAF is a
glycosylphosphatidyl inositol-anchored complement regulatory protein found on
most cell surfaces. It functions to protect cells from complement attack. The
cryo-electron microscopy reconstructions of echovirus 7 complexed with DAF show
that the DAF-binding regions are located close to the icosahedral twofold axes,
in contrast to other enterovirus complexes where the viral canyon is the
receptor binding site. This novel receptor binding position suggests that DAF is
important for the attachment of viral particles to host cells, but probably not
for initiating viral uncoating, as is the case with canyon-binding receptors.
Thus, a different cell entry mechanism must be used for enteroviruses that bind
DAF.
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Selected figure(s)
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Figure 1.
Fig 1. Diagrammatic structure of DAF. The green ellipses
represent the SCR domains. The yellow spheres are O-linked and
the orange spheres are N-linked carbohydrate moieties. GPI,
glycosylphosphatidylinositol.
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Figure 2.
Fig 2. Surface representation of cryoEM image
reconstructions. Comparison of ECHO7 (c) with complexes of ECHO7
and DAF fragments shows (in red) the density attributed to DAF.
An icosahedral asymmetric unit is outlined in black in c.
Comparisons of the reconstruction of ECHO7 complexed with either
DAF1234 (a) or DAF234 (b) shows that SCR domain 1 is located
near the threefold axes. The surface contour is at 1  for each
complex.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.M.Sandager,
J.L.Nugent,
W.L.Schulz,
R.P.Messner,
and
P.E.Tam
(2008).
Interactions between multiple genetic determinants in the 5' UTR and VP1 capsid control pathogenesis of chronic post-viral myopathy caused by coxsackievirus B1.
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Virology,
372,
35-47.
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S.Hafenstein,
V.D.Bowman,
P.R.Chipman,
C.M.Bator Kelly,
F.Lin,
M.E.Medof,
and
M.G.Rossmann
(2007).
Interaction of decay-accelerating factor with coxsackievirus B3.
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J Virol,
81,
12927-12935.
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PDB codes:
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S.K.Lau,
C.C.Yip,
H.W.Tsoi,
R.A.Lee,
L.Y.So,
Y.L.Lau,
K.H.Chan,
P.C.Woo,
and
K.Y.Yuen
(2007).
Clinical features and complete genome characterization of a distinct human rhinovirus (HRV) genetic cluster, probably representing a previously undetected HRV species, HRV-C, associated with acute respiratory illness in children.
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J Clin Microbiol,
45,
3655-3664.
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E.Pokidysheva,
Y.Zhang,
A.J.Battisti,
C.M.Bator-Kelly,
P.R.Chipman,
C.Xiao,
G.G.Gregorio,
W.A.Hendrickson,
R.J.Kuhn,
and
M.G.Rossmann
(2006).
Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN.
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Cell,
124,
485-493.
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PDB code:
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P.E.Tam
(2006).
Coxsackievirus myocarditis: interplay between virus and host in the pathogenesis of heart disease.
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Viral Immunol,
19,
133-146.
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A.M.Milstone,
J.Petrella,
M.D.Sanchez,
M.Mahmud,
J.C.Whitbeck,
and
J.M.Bergelson
(2005).
Interaction with coxsackievirus and adenovirus receptor, but not with decay-accelerating factor (DAF), induces A-particle formation in a DAF-binding coxsackievirus B3 isolate.
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J Virol,
79,
655-660.
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I.G.Goodfellow,
D.J.Evans,
A.M.Blom,
D.Kerrigan,
J.S.Miners,
B.P.Morgan,
and
O.B.Spiller
(2005).
Inhibition of coxsackie B virus infection by soluble forms of its receptors: binding affinities, altered particle formation, and competition with cellular receptors.
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J Virol,
79,
12016-12024.
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M.Dan,
and
J.K.Chantler
(2005).
A genetically engineered attenuated coxsackievirus B3 strain protects mice against lethal infection.
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J Virol,
79,
9285-9295.
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C.Xiao,
T.J.Tuthill,
C.M.Bator Kelly,
L.J.Challinor,
P.R.Chipman,
R.A.Killington,
D.J.Rowlands,
A.Craig,
and
M.G.Rossmann
(2004).
Discrimination among rhinovirus serotypes for a variant ICAM-1 receptor molecule.
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J Virol,
78,
10034-10044.
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E.S.Johansson,
L.Xing,
R.H.Cheng,
and
D.R.Shafren
(2004).
Enhanced cellular receptor usage by a bioselected variant of coxsackievirus a21.
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J Virol,
78,
12603-12612.
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E.Stadnick,
M.Dan,
A.Sadeghi,
and
J.K.Chantler
(2004).
Attenuating mutations in coxsackievirus B3 map to a conformational epitope that comprises the puff region of VP2 and the knob of VP3.
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J Virol,
78,
13987-14002.
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H.Duque,
M.LaRocco,
W.T.Golde,
and
B.Baxt
(2004).
Interactions of foot-and-mouth disease virus with soluble bovine alphaVbeta3 and alphaVbeta6 integrins.
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J Virol,
78,
9773-9781.
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N.G.Newcombe,
E.S.Johansson,
G.Au,
A.M.Lindberg,
R.D.Barry,
and
D.R.Shafren
(2004).
Enterovirus capsid interactions with decay-accelerating factor mediate lytic cell infection.
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J Virol,
78,
1431-1439.
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N.G.Newcombe,
L.G.Beagley,
D.Christiansen,
B.E.Loveland,
E.S.Johansson,
K.W.Beagley,
R.D.Barry,
and
D.R.Shafren
(2004).
Novel role for decay-accelerating factor in coxsackievirus A21-mediated cell infectivity.
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J Virol,
78,
12677-12682.
|
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S.E.Myers,
L.Brewer,
D.P.Shaw,
W.H.Greene,
B.C.Love,
B.Hering,
O.B.Spiller,
and
M.K.Njenga
(2004).
Prevalent human coxsackie B-5 virus infects porcine islet cells primarily using the coxsackie-adenovirus receptor.
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Xenotransplantation,
11,
536-546.
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S.Hudault,
O.B.Spiller,
B.P.Morgan,
and
A.L.Servin
(2004).
Human diffusely adhering Escherichia coli expressing Afa/Dr adhesins that use human CD55 (decay-accelerating factor) as a receptor does not bind the rodent and pig analogues of CD55.
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Infect Immun,
72,
4859-4863.
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E.E.Fry,
N.J.Knowles,
J.W.Newman,
G.Wilsden,
Z.Rao,
A.M.King,
and
D.I.Stuart
(2003).
Crystal structure of Swine vesicular disease virus and implications for host adaptation.
|
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J Virol,
77,
5475-5486.
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PDB code:
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Y.He,
S.Mueller,
P.R.Chipman,
C.M.Bator,
X.Peng,
V.D.Bowman,
S.Mukhopadhyay,
E.Wimmer,
R.J.Kuhn,
and
M.G.Rossmann
(2003).
Complexes of poliovirus serotypes with their common cellular receptor, CD155.
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J Virol,
77,
4827-4835.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
