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Contents |
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285 a.a.
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252 a.a.
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238 a.a.
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29 a.a.
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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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The refined structure of a picornavirus inhibitor currently in clinical trials, When complexed with human rhinovirus 16
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Authors
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S.Chakravarty,
C.M.Bator,
D.C.Pevear,
G.D.Diana,
M.G.Rossmann.
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Ref.
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to be published ...
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Secondary reference #1
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Title
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Analysis of three structurally related antiviral compounds in complex with human rhinovirus 16.
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Authors
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A.T.Hadfield,
G.D.Diana,
M.G.Rossmann.
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Ref.
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Proc Natl Acad Sci U S A, 1999,
96,
14730-14735.
[DOI no: ]
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PubMed id
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Figure 4.
Fig. 4. Difference in binding of compounds 1 and 2
compared with compound 3. (A) Electron density for compound 1,
contoured at a 1.5  level.
Compound 1 is shown in purple bonds and compound 3 is shown as
black bonds. (B) Ball-and-stick representation of compound 1
(black sticks) and compound 3 (green sticks) viewed from (Lower)
looking from the compound toward the outside of the virion and
(Upper) looking from the compound toward the center of the
virion. The insert localizes the site with respect to the
symmetry axes in the icosahedral asymmetric unit. The labels X
and Y define opposite sides of the WIN binding pocket. Side
chains that are within 4 Å of the compounds are shown in
thin black bonds. Water molecules are shown as red spheres with
their hydrogen bonding environment in ball-and-stick
representation. Compound 4 is overlaid in green dotted lines.
The figure was prepared by using MOLSCRIPT (43).
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Figure 5.
Fig. 5. The same as Fig. 4B, but showing the comparison
of compound binding sites in HRV16 and HRV14. Ball-and-stick
representation of compound 1 (white sticks) bound to HRV16 (side
chains within 4 Å shown in thin black bonds). The binding
pocket of HRV14 with two compounds bound is superimposed.
Compound 5 is shown in black ball-and-stick representation,
while compound 6 is shown as dashed magenta lines (side chains
within 4 Å of the compounds shown in magenta bonds). The
comparison is based on a least-squares fit between C[  ]atoms
in the  -barrel of
VP1.
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Secondary reference #2
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Title
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The refined structure of human rhinovirus 16 at 2.15 a resolution: implications for the viral life cycle.
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Authors
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A.T.Hadfield,
W.Lee,
R.Zhao,
M.A.Oliveira,
I.Minor,
R.R.Rueckert,
M.G.Rossmann.
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Ref.
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Structure, 1997,
5,
427-441.
[DOI no: ]
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PubMed id
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Figure 6.
Figure 6. A schematic diagram representing VP1 of HRV16,
showing the binding site of the pocket factor (shown in
ball-and-stick representation) and the WIN antiviral compounds
(shown in pale blue). A cation on the fivefold axis is shown in
yellow. The N termini of VP1, VP3 and VP4 also interact around
the fivefold axis. One copy of each of VP1 and the N termini of
VP3 and VP4 are shown as blue, red and green ribbon diagrams,
respectively. The myristylated N terminus of VP4 is labelled
(MYR). (The diagram was created using MOLSCRIPT [64].)
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #3
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Title
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The structure of human rhinovirus 16.
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Authors
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M.A.Oliveira,
R.Zhao,
W.M.Lee,
M.J.Kremer,
I.Minor,
R.R.Rueckert,
G.D.Diana,
D.C.Pevear,
F.J.Dutko,
M.A.Mckinlay.
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Ref.
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Structure, 1993,
1,
51-68.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Diagrammatic view of picor-
navirus with enlargementofone icosa-
hedral asymmetric unit showing the
outline of the canyon and the entrance
to the WIN pocket. The terms 'north'
(top) and 'south' rims of the canyon
refer to this standard oientation. The
6S protomeric assembly unit (which dif-
fers from the geometric definitionof the
asymmetric unit) is shown in heay out-
line on the icosahedron.
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Figure 4.
Fig. 4. (a) Roadmap showing the amino acids covering the surface of
HRV16. The boundary of the canyon is shown, arbitrar~ily assumed to be
at a plane height of 139A measured along a two-fold axis, as well as
the shaded footprint of the ICAM-1 receptor molecule derived from
cryoelectron microscopy [18]. The footprint was determined as those
residues which have any atom within 4.0 A of any atom of the modeled
receptor molecule. (b) Surface topology of HRV16. Colors represent
relative distances from the viral center in planes perpendicular to a
two-fold axis, with blue being the lowest surface depression and white
the highest surface features. ]Figures computed by the program VSurf
and prepared by JY Sgro, University of Wisconsin, Madison.]
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #4
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Title
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Structure of a human rhinovirus complexed with its receptor molecule.
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Authors
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N.H.Olson,
P.R.Kolatkar,
M.A.Oliveira,
R.H.Cheng,
J.M.Greve,
A.Mcclelland,
T.S.Baker,
M.G.Rossmann.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
507-511.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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A comparison of the anti-Rhinoviral drug binding pocket in hrv14 and hrv1a.
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Authors
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K.H.Kim,
P.Willingmann,
Z.X.Gong,
M.J.Kremer,
M.S.Chapman,
I.Minor,
M.A.Oliveira,
M.G.Rossmann,
K.Andries,
G.D.Diana.
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Ref.
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J Mol Biol, 1993,
230,
206-227.
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PubMed id
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Secondary reference #6
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Title
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Crystal structure of human rhinovirus serotype 1a (hrv1a).
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Authors
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S.S.Kim,
T.J.Smith,
M.S.Chapman,
M.C.Rossmann,
D.C.Pevear,
F.J.Dutko,
P.J.Felock,
G.D.Diana,
M.A.Mckinlay.
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Ref.
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J Mol Biol, 1989,
210,
91.
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PubMed id
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Secondary reference #7
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Title
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The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating.
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Authors
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T.J.Smith,
M.J.Kremer,
M.Luo,
G.Vriend,
E.Arnold,
G.Kamer,
M.G.Rossmann,
M.A.Mckinlay,
G.D.Diana,
M.J.Otto.
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Ref.
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Science, 1986,
233,
1286-1293.
[DOI no: ]
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PubMed id
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Secondary reference #8
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Title
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Structure of a human common cold virus and functional relationship to other picornaviruses.
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Authors
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M.G.Rossmann,
E.Arnold,
J.W.Erickson,
E.A.Frankenberger,
J.P.Griffith,
H.J.Hecht,
J.E.Johnson,
G.Kamer,
M.Luo,
A.G.Mosser.
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Ref.
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Nature, 1985,
317,
145-153.
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PubMed id
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