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Contents |
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* Residue conservation analysis
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DOI no:
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Science
286:1579-1583
(1999)
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PubMed id:
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Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR.
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M.C.Bewley,
K.Springer,
Y.B.Zhang,
P.Freimuth,
J.M.Flanagan.
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ABSTRACT
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Binding of virus particles to specific host cell surface receptors is known to
be an obligatory step in infection even though the molecular basis for these
interactions is not well characterized. The crystal structure of the adenovirus
fiber knob domain in complex with domain I of its human cellular receptor,
coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed
loops on knob contact one face of CAR, forming a high-affinity complex. Topology
mismatches between interacting surfaces create interfacial solvent-filled
cavities and channels that may be targets for antiviral drug therapy. The
structure identifies key determinants of binding specificity, which may suggest
ways to modify the tropism of adenovirus-based gene therapy vectors.
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Selected figure(s)
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Figure 2.
Fig. 2. A molecular surface representation of the interface in
the Ad12 knob-CAR D1 complex. (A) Sequence conservation surface
diagram of two knob monomers viewed at the CAR interface. The
molecules are colored on a sliding scale from white (conserved)
to red (nonconserved). Conservation analysis was based on an
alignment of all human Ad knob sequences available in GenBank. A
white strip of conservation transects the surface of the
molecule. Upon binding, the CAR D1 molecule occludes the
conserved strip on Ad12 knob. (B) Surface diagram of two
adjacent Ad12 knob monomers shown in the same view as (A). The
molecules are colored on a sliding scale from yellow (contact)
to red (no contact). Atoms in contact with CAR D1 are shared
between monomers. (C) Surface diagram of CAR D1. The molecules
are colored on a sliding scale from magenta (contact) to cyan
(no contact). This figure was generated with GRASP (30).
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Figure 3.
Fig. 3. CPK model of the region around the cavity. The three
consecutive proline residues in Ad12 knob partially shape the
cavity, which is colored magenta. The AB loop, whose carbon
atoms are colored yellow, lines one side of the cavity. The
carbon atoms from the remainder of the monomer are colored red,
those of the second knob monomer, green, and those of CAR D1,
cyan. All oxygen and nitrogen atoms are colored light red and
blue, respectively. The cavity is lined with atoms from residues
 ,
 (backbone),
 (side),
V448 (side),  (backbone),
V450, L455 (side), Q535 (side), P573 (side), and S575 (side)
from one Ad12 knob; S514 (backbone), A515 (backbone),  (side),
N520 (side), A524 (main), E523, K525, and S526 (side) from the
other Ad12 knob; and L39 (side), K47 (backbone), V48 (backbone),
D49, Q50, V51, and K102 (side) from CAR. The underlined residues
are conserved or similar in all CAR-binding Ad serotypes.
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The above figures are
reprinted
by permission from the AAAs:
Science
(1999,
286,
1579-1583)
copyright 1999.
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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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PDB code:
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PDB codes:
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A.E.Prota,
J.A.Campbell,
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PDB code:
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Crystal structure of reovirus attachment protein sigma1 reveals evolutionary relationship to adenovirus fiber.
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EMBO J,
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PDB code:
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J.Petrella,
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A zebrafish coxsackievirus and adenovirus receptor homologue interacts with coxsackie B virus and adenovirus.
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J Virol,
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J Virol,
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J Virol,
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J Virol,
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Adenovirus type 37 uses sialic acid as a cellular receptor on Chang C cells.
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J Virol,
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Cell,
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Efficient adenovirus-mediated gene transfer into primary T cells and thymocytes in a new coxsackie/adenovirus receptor transgenic model.
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J Virol,
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Adenoviral transduction efficiency of ovarian cancer cells can be limited by loss of integrin beta3 subunit expression and increased by reconstitution of integrin alphavbeta3.
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Hum Gene Ther,
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(2001).
Herpes simplex virus glycoprotein D bound to the human receptor HveA.
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Mol Cell,
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PDB codes:
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|
C.J.Cohen,
J.T.Shieh,
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The coxsackievirus and adenovirus receptor is a transmembrane component of the tight junction.
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Proc Natl Acad Sci U S A,
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Structural analysis of a fiber-pseudotyped adenovirus with ocular tropism suggests differential modes of cell receptor interactions.
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J Virol,
75,
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E.Davison,
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Adenovirus type 5 uptake by lung adenocarcinoma cells in culture correlates with Ad5 fibre binding is mediated by alpha(v)beta1 integrin and can be modulated by changes in beta1 integrin function.
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J Gene Med,
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Adenovirus type 9 fiber knob binds to the coxsackie B virus-adenovirus receptor (CAR) with lower affinity than fiber knobs of other CAR-binding adenovirus serotypes.
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J Virol,
75,
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J.L.Jakubczak,
M.L.Rollence,
D.A.Stewart,
J.D.Jafari,
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Adenovirus type 5 viral particles pseudotyped with mutagenized fiber proteins show diminished infectivity of coxsackie B-adenovirus receptor-bearing cells.
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J Virol,
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J.Nalbantoglu,
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Muscle-specific overexpression of the adenovirus primary receptor CAR overcomes low efficiency of gene transfer to mature skeletal muscle.
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J Virol,
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Gut,
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M.C.Dechecchi,
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Heparan sulfate glycosaminoglycans are receptors sufficient to mediate the initial binding of adenovirus types 2 and 5.
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J Virol,
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Drug Discov Today,
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W.van't Hof,
S.M.Yi,
M.K.Schroth,
J.Zabner,
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Apical localization of the coxsackie-adenovirus receptor by glycosyl-phosphatidylinositol modification is sufficient for adenovirus-mediated gene transfer through the apical surface of human airway epithelia.
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J Virol,
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S.D.Carson
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Receptor for the group B coxsackieviruses and adenoviruses: CAR.
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Interaction of coxsackievirus B3 with the full length coxsackievirus-adenovirus receptor.
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Nat Struct Biol,
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PDB code:
|
|
|
|
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|
|
C.Soudais,
S.Boutin,
S.S.Hong,
M.Chillon,
O.Danos,
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Canine adenovirus type 2 attachment and internalization: coxsackievirus-adenovirus receptor, alternative receptors, and an RGD-independent pathway.
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J Virol,
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Dependence of adenovirus infectivity on length of the fiber shaft domain.
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J Virol,
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G.R.Nemerow
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Trends Microbiol,
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Ectodomain of coxsackievirus and adenovirus receptor genetically fused to epidermal growth factor mediates adenovirus targeting to epidermal growth factor receptor-positive cells.
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J Virol,
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Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution.
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| |
Structure,
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|
PDB codes:
|
|
|
|
|
|
|
|
N.E.Bowles,
and
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(2000).
Molecular Aspects of Myocarditis.
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Curr Infect Dis Rep,
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(2000).
Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates.
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| |
Structure,
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|
|
|
PDB codes:
|
|
|
|
|
|
|
|
Y.Chen,
D.C.Yu,
D.Charlton,
and
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Pre-existent adenovirus antibody inhibits systemic toxicity and antitumor activity of CN706 in the nude mouse LNCaP xenograft model: implications and proposals for human therapy.
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Transgenic expression of the coxsackie/adenovirus receptor enables adenoviral-mediated gene delivery in naive T cells.
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Proc Natl Acad Sci U S A,
97,
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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
code is
shown on the right.
|
 |
Links
