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PDBsum entry 1mec
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274 a.a.
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256 a.a.
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231 a.a.
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62 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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Conformational variability of a picornavirus capsid: ph-Dependent structural changes of mengo virus related to its host receptor attachment site and disassembly.
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Authors
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S.Kim,
U.Boege,
S.Krishnaswamy,
I.Minor,
T.J.Smith,
M.Luo,
D.G.Scraba,
M.G.Rossmann.
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Ref.
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Virology, 1990,
175,
176-190.
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PubMed id
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Abstract
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The structure of Mengo virus had been determined from crystals grown in the
presence of 100 mM phosphate buffer at pH 7.4. It is shown that Mengo virus is
poorly infectious at the phosphate concentration similar to that in which it was
crystallized. Maximal infectivity is achieved at 10 mM phosphate or less in
physiological saline. The phosphate effect is ameliorated when the pH is lowered
to 4.6. Although it has not been possible to study the crystal structure of the
virus at low phosphate concentrations, it is shown that increasing the Cl-
concentration at pH 6.2 or decreasing the pH to 4.6 causes substantial
conformational changes confined to the "pit," a deep surface depression. These
structural changes involve a movement of the "FMDV loop" (GH loop) in VP1, an
ordering of the "VP3 loop" (GH loop in VP3) between 3176 and 3182, the
displacement of a bound phosphate near the "FMDV loop" (GH loop in VP1), and
movement of the carboxy terminus of VP2. The changes in conformation are
correlated with the dissociation of the virion into pentamers at pH 6.2 and 150
mM Cl-. The localization of the conformational changes and the correlated role
of the phosphate in controlling infectivity support the hypothesis that the
"pit" is the receptor attachment site.
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Secondary reference #1
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Title
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Structural refinement and analysis of mengo virus.
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Authors
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S.Krishnaswamy,
M.G.Rossmann.
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Ref.
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J Mol Biol, 1990,
211,
803-844.
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PubMed id
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Secondary reference #2
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Title
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Structure determination of mengo virus.
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Authors
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M.Luo,
G.Vriend,
G.Kamer,
M.G.Rossmann.
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Ref.
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Acta Crystallogr B, 1989,
45,
85-92.
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PubMed id
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Secondary reference #3
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Title
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The atomic structure of mengo virus at 3.0 a resolution.
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Authors
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M.Luo,
G.Vriend,
G.Kamer,
I.Minor,
E.Arnold,
M.G.Rossmann,
U.Boege,
D.G.Scraba,
G.M.Duke,
A.C.Palmenberg.
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Ref.
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Science, 1987,
235,
182-191.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Implications of the picornavirus capsid structure for polyprotein processing.
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Authors
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E.Arnold,
M.Luo,
G.Vriend,
M.G.Rossmann,
A.C.Palmenberg,
G.D.Parks,
M.J.Nicklin,
E.Wimmer.
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Ref.
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Proc Natl Acad Sci U S A, 1987,
84,
21-25.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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The structure of a human common cold virus (rhinovirus 14) and its evolutionary relations to other viruses
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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,
G.Vriend,
A.G.Mosser,
A.C.Palmenberg,
R.R.Rueckert,
B.Sherry.
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Ref.
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chem scr ,sect b, 1986,
26,
313.
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Secondary reference #6
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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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Secondary reference #7
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Title
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Picornaviruses of two different genera have similar structures.
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Authors
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M.Luo,
E.Arnold,
J.W.Erickson,
M.G.Rossmann,
U.Boege,
D.G.Scraba.
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Ref.
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J Mol Biol, 1984,
180,
703-714.
[DOI no: ]
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PubMed id
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Figure 1.
MING Luo, EDWARD ARNOLD, JOHN W. ERICKSON?, MICHAEL G. ROSSMANN
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Figure 7.
FIG. 7. Cross-rotation functions between Mengo and rhinovirus crystals. (a) Mengo stationary
(compund 1) with rhino (compoun 2) rotted by -6. (b) Rhino tationary (compound 1) with
Mengo (compound 2) rotated by -6. R = 0 corresponds approximately to the mean value of the
rotation functions.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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