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PDBsum entry 1eaj
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Virus/viral protein receptor
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PDB id
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1eaj
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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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Dimeric structure of the coxsackievirus and adenovirus receptor d1 domain at 1.7 a resolution.
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Authors
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M.J.Van raaij,
E.Chouin,
H.Van der zandt,
J.M.Bergelson,
S.Cusack.
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Ref.
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Structure, 2000,
8,
1147-1155.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: The coxsackievirus and adenovirus receptor (CAR) comprises two
extracellular immunoglobulin domains, a transmembrane helix and a C-terminal
intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is
necessary and sufficient for adenovirus binding, whereas the site of
coxsackievirus attachment has not yet been localized. The normal cellular role
of CAR is currently unknown, although CAR was recently proposed to function as a
homophilic cell adhesion molecule. RESULTS: The human CAR D1 domain was
bacterially expressed and crystallized. The structure was solved by molecular
replacement using the structure of CAR D1 bound to the adenovirus type 12 fiber
head and refined to 1.7 A resolution, including individual anisotropic
temperature factors. The two CAR D1 structures are virtually identical, apart
from the BC, C"D, and FG loops that are involved both in fiber head binding
and homodimerization in the crystal. Analytical equilibrium ultracentrifugation
shows that a dimer also exists in solution, with a dissociation constant of 16
microM. CONCLUSIONS: The CAR D1 domain forms homodimers in the crystal using the
same GFCC'C" surface that interacts with the adenovirus fiber head. The
homodimer is very similar to the CD2 D1-CD58 D1 heterodimer. CAR D1 also forms
dimers in solution with a dissociation constant typical of other cell adhesion
complexes. These results are consistent with reports that CAR may function
physiologically as a homophilic cell adhesion molecule in the developing mouse
brain. Adenovirus may thus have recruited an existing and conserved interaction
surface of CAR to use for its own cell attachment.
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Figure 3.
Figure 3. The CAR D1 Homodimer(a) The CAR D1 dimer viewed
down the noncrystallographic dyad. Monomer A is colored blue,
and B is yellow. Residues involved in direct hydrogen bonds
between the two monomers are shown in orange and labeled for
monomer A. The N- and C-termini are labeled and the approximate
position of the noncrystallographic dyad is indicated.(b)
Surface representation of monomer A in blue. The surface that
gets buried upon homodimer formation with monomer B is shown in
yellow. Residues involved in dimer interactions are indicated.
This figure was prepared using the program GRASP [48]
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2000,
8,
1147-1155)
copyright 2000.
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