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* Residue conservation analysis
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PDB id:
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Viral protein/receptor
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Title:
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Ad37 fibre head in complex with car d1
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Structure:
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Fiber protein. Chain: a. Fragment: fibre head, residues 177-365. Synonym: adenovirus 37 fibre head. Engineered: yes. Coxsackievirus and adenovirus receptor. Chain: b. Fragment: domain d1, residues 15-140. Synonym: coxsackievirus b-adenovirus receptor, hcar, cvb3-binding
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Source:
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Human adenovirus d37. Organism_taxid: 52275. Strain: type 37. Expressed in: escherichia coli. Expression_system_taxid: 511693. Homo sapiens. Human. Organism_taxid: 9606. Expression_system_taxid: 562.
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Biol. unit:
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Hexamer (from PDB file)
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Resolution:
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1.50Å
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R-factor:
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0.149
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R-free:
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0.169
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Authors:
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E.Seiradake,H.Lortat-Jacob,O.Billet,E.J.Kremer,S.Cusack
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Key ref:
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E.Seiradake
et al.
(2006).
Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.
J Biol Chem,
281,
33704-33716.
PubMed id:
DOI:
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Date:
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08-Aug-06
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Release date:
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29-Aug-06
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PROCHECK
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Headers
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References
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DOI no:
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J Biol Chem
281:33704-33716
(2006)
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PubMed id:
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Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor.
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E.Seiradake,
H.Lortat-Jacob,
O.Billet,
E.J.Kremer,
S.Cusack.
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ABSTRACT
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Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and
adenovirus receptor (CAR), although the binding residues are not strictly
conserved. To understand this further, we determined the crystal structures of
canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37
(HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively.
Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the
overall topology of the interaction is conserved but that the interfaces differ
in number and identity of interacting residues, shape complementarity, and
degree of conformational adaptation. Using surface plasmon resonance, we
characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and
HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest
direct interactions, with the reverse being true for HAd37. Moreover, we found
that conserved interactions can have a minor contribution, whereas
serotype-specific interactions can be essential. These results are discussed in
the light of virus evolution and design of adenovirus vectors for gene transfer.
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Selected figure(s)
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Figure 2.
FIGURE 2. Cartoon representations of adenovirus fiber heads
in complex with CAR D1. HAd12, HAd37, and CAV-2 fiber heads are
colored blue, pink, and yellow, respectively. CAR D1 is in
green. A, top view of the structure of HAd12 fiber head in
complex with CAR D1 (13). B, as A, but HAd37 fiber head. C, as A
and B, but CAV-2 fiber head. D, part of the binding interface
between HAd12 fiber head and CAR D1 showing some key interacting
residues. E, equivalent region of interface between HAd37 fiber
head and CAR D1 showing conservation of the interactions and
additional unique interactions provided by HAd37 Glu^351 from
the IJ loop. F, same region of the CAV-2 fiber head and CAR D1
interface showing equivalent interactions made by sometimes
different fiber residues. Hydrogen bonds are shown in dotted
lines. Residues marked with an asterisk are not fully
represented for clarity.
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Figure 6.
FIGURE 6. SPR sensorgrams of wild type and mutant
adenovirus fiber heads binding to immobilized CAR D1. A, wild
type HAd37 fiber head; B, HAd37 fiber head mutant S299A; C,
HAd37 fiber head mutant E351A; D, wild type CAV-2 fiber head; E,
CAV-2 fiber head mutant T441A; F, CAV-2 fiber head mutant R384E;
G, CAV-2 fiber head mutant R515A; H, CAV-2 fiber head mutant
G370D; I, CAV-2 fiber head mutant R384A. , results calculated
from the sensorgrams. The S.E. did not exceed 15% of the K[d].
,
Lortat-Jacob et al. (51) using the same experimental set-up and
CAR construct as in this work. , Kirby et al. (67)
using a longer CAR construct.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
33704-33716)
copyright 2006.
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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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D.Henaff,
S.Salinas,
and
E.J.Kremer
(2011).
An adenovirus traffic update: from receptor engagement to the nuclear pore.
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Future Microbiol,
6,
179-192.
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K.Cupelli,
S.Müller,
B.D.Persson,
M.Jost,
N.Arnberg,
and
T.Stehle
(2010).
Structure of adenovirus type 21 knob in complex with CD46 reveals key differences in receptor contacts among species B adenoviruses.
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J Virol,
84,
3189-3200.
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PDB codes:
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E.Seiradake,
A.C.von Philipsborn,
M.Henry,
M.Fritz,
H.Lortat-Jacob,
M.Jamin,
W.Hemrika,
M.Bastmeyer,
S.Cusack,
and
A.A.McCarthy
(2009).
Structure and functional relevance of the Slit2 homodimerization domain.
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EMBO Rep,
10,
736-741.
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PDB code:
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E.Seiradake,
D.Henaff,
H.Wodrich,
O.Billet,
M.Perreau,
C.Hippert,
F.Mennechet,
G.Schoehn,
H.Lortat-Jacob,
H.Dreja,
S.Ibanes,
V.Kalatzis,
J.P.Wang,
R.W.Finberg,
S.Cusack,
and
E.J.Kremer
(2009).
The cell adhesion molecule "CAR" and sialic acid on human erythrocytes influence adenovirus in vivo biodistribution.
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PLoS Pathog,
5,
e1000277.
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PDB codes:
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J.Rebetz,
M.Na,
C.Su,
B.Holmqvist,
A.Edqvist,
C.Nyberg,
B.Widegren,
L.G.Salford,
H.O.Sjögren,
N.Arnberg,
Q.Qian,
and
X.Fan
(2009).
Fiber mediated receptor masking in non-infected bystander cells restricts adenovirus cell killing effect but promotes adenovirus host co-existence.
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PLoS One,
4,
e8484.
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S.Salinas,
L.G.Bilsland,
D.Henaff,
A.E.Weston,
A.Keriel,
G.Schiavo,
and
E.J.Kremer
(2009).
CAR-associated vesicular transport of an adenovirus in motor neuron axons.
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PLoS Pathog,
5,
e1000442.
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T.Stehle,
and
J.M.Casasnovas
(2009).
Specificity switching in virus-receptor complexes.
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Curr Opin Struct Biol,
19,
181-188.
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D.Hatherley,
S.C.Graham,
J.Turner,
K.Harlos,
D.I.Stuart,
and
A.N.Barclay
(2008).
Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47.
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Mol Cell,
31,
266-277.
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PDB codes:
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G.Schoehn,
M.El Bakkouri,
C.M.Fabry,
O.Billet,
L.F.Estrozi,
L.Le,
D.T.Curiel,
A.V.Kajava,
R.W.Ruigrok,
and
E.J.Kremer
(2008).
Three-dimensional structure of canine adenovirus serotype 2 capsid.
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J Virol,
82,
3192-3203.
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K.Sirikanchana,
J.L.Shisler,
and
B.J.Mariñas
(2008).
Effect of exposure to UV-C irradiation and monochloramine on adenovirus serotype 2 early protein expression and DNA replication.
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Appl Environ Microbiol,
74,
3774-3782.
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M.A.Shannon,
P.W.Bohn,
M.Elimelech,
J.G.Georgiadis,
B.J.Mariñas,
and
A.M.Mayes
(2008).
Science and technology for water purification in the coming decades.
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Nature,
452,
301-310.
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K.J.Excoffon,
N.Gansemer,
G.Traver,
and
J.Zabner
(2007).
Functional effects of coxsackievirus and adenovirus receptor glycosylation on homophilic adhesion and adenoviral infection.
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J Virol,
81,
5573-5578.
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M.Perreau,
F.Mennechet,
N.Serratrice,
J.N.Glasgow,
D.T.Curiel,
H.Wodrich,
and
E.J.Kremer
(2007).
Contrasting effects of human, canine, and hybrid adenovirus vectors on the phenotypical and functional maturation of human dendritic cells: implications for clinical efficacy.
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J Virol,
81,
3272-3284.
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M.Perreau,
M.C.Guérin,
C.Drouet,
and
E.J.Kremer
(2007).
Interactions between human plasma components and a xenogenic adenovirus vector: reduced immunogenicity during gene transfer.
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Mol Ther,
15,
1998-2007.
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R.J.Ossiboff,
and
J.S.Parker
(2007).
Identification of regions and residues in feline junctional adhesion molecule required for feline calicivirus binding and infection.
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J Virol,
81,
13608-13621.
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R.L.Rich,
and
D.G.Myszka
(2007).
Survey of the year 2006 commercial optical biosensor literature.
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J Mol Recognit,
20,
300-366.
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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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}
}
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