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PDBsum entry 1dgi
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Virus/receptor
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PDB id
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1dgi
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Contents |
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301 a.a.*
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288 a.a.*
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268 a.a.*
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235 a.a.*
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63 a.a.*
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* C-alpha coords only
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References listed in PDB file
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Key reference
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Title
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Interaction of the poliovirus receptor with poliovirus.
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Authors
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Y.He,
V.D.Bowman,
S.Mueller,
C.M.Bator,
J.Bella,
X.Peng,
T.S.Baker,
E.Wimmer,
R.J.Kuhn,
M.G.Rossmann.
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Ref.
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Proc Natl Acad Sci U S A, 2000,
97,
79-84.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the extracellular, three-domain poliovirus receptor (CD155)
complexed with poliovirus (serotype 1) has been determined to 22-A resolution by
means of cryo-electron microscopy and three-dimensional image-reconstruction
techniques. Density corresponding to the receptor was isolated in a difference
electron density map and fitted with known structures, homologous to those of
the three individual CD155 Ig-like domains. The fit was confirmed by the
location of carbohydrate moieties in the CD155 glycoprotein, the conserved
properties of elbow angles in the structures of cell surface molecules with
Ig-like folds, and the concordance with prior results of CD155 and poliovirus
mutagenesis. CD155 binds in the poliovirus "canyon" and has a
footprint similar to that of the intercellular adhesion molecule-1 receptor on
human rhinoviruses. However, the orientation of the long, slender CD155 molecule
relative to the poliovirus surface is quite different from the orientation of
intercellular adhesion molecule-1 on rhinoviruses. In addition, the residues
that provide specificity of recognition differ for the two receptors. The
principal feature of receptor binding common to these two picornaviruses is the
site in the canyon at which binding occurs. This site may be a trigger for
initiation of the subsequent uncoating step required for viral infection.
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Figure 1.
Fig. 1. Comparison of the mature structures of ICAM-1,
the receptor for the major group of rhinoviruses, with the human
PV receptor (hCD155), the monkey PV receptor (mCD155), and the
murine poliovirus receptor-related protein 2 (mPRR2). Sites of
glycosylation are indicated by shaded circles. The number of
amino acids is shown for each domain.
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Figure 6.
Fig. 6. The footprint of the CD155 on the PV surface,
defined by those residues on the viral surface that have any
atoms within 4 Å of any atom in the receptor. (Inset) One
icosahedral asymmetric unit with the footprint outlined and the
limits of the canyon. (Left) The footprint on the virus (the
canyon has a black outline). (Right) The residues of CD155 in
contact with the viral surface. Each residue is colored in
accordance with its chemical properties: green, hydrophobic;
yellow, hydrophilic; red, acidic; and blue, basic.
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Secondary reference #1
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Title
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The structure of the two amino-Terminal domains of human icam-1 suggests how it functions as a rhinovirus receptor and as an lfa-1 integrin ligand.
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Authors
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J.Bella,
P.R.Kolatkar,
C.W.Marlor,
J.M.Greve,
M.G.Rossmann.
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Ref.
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Proc Natl Acad Sci U S A, 1998,
95,
4140-4145.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. A diagram of an ICAM-1 molecule showing sites of
glycosylation (lollipop-shaped structures) and the approximate
location of binding sites of LFA-1, Mac-1, human rhinoviruses,
fibrinogen, and Plasmodium falciparum-infected erythrocytes
(PFIE).
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Figure 5.
Fig. 5. Ribbon diagram showing docking of the I-domain of
LFA-1 (green) with domain D1 of mutICAM-1 (orange). Coordination
of the metal ion (purple) on the I-domain is completed by Glu-34
(white) on the  -strand C of
mutICAM-1. Additional residues of the I-domain (36) and of
ICAM-1 (24) considered important for binding are shown in green
and yellow, respectively.
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Secondary reference #2
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Title
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Three-Dimensional structure of poliovirus at 2.9 a resolution.
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Authors
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J.M.Hogle,
M.Chow,
D.J.Filman.
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Ref.
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Science, 1985,
229,
1358-1365.
[DOI no: ]
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PubMed id
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Headers
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