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PDBsum entry 3j3o
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Virus/immune system
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PDB id
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3j3o
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Contents |
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219 a.a.*
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220 a.a.*
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5 a.a.*
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283 a.a.*
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268 a.a.*
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235 a.a.*
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60 a.a.*
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* C-alpha coords only
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PDB id:
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| Name: |
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Virus/immune system
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Title:
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Conformational shift of a major poliovirus antigen confirmed by immuno-cryogenic electron microscopy: 160s poliovirus and c3-fab complex
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Structure:
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C3 antibody, light chain. Chain: l. Fragment: fab. C3 antibody, heavy chain. Chain: h. Fragment: fab. Unknown peptide. Chain: 0. Protein vp1.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Unidentified. Organism_taxid: 32644. Human poliovirus 1. Organism_taxid: 12081. Strain: mahoney. Strain: mahoney
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Authors:
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J.Lin,N.Cheng,J.M.Hogle,A.C.Steven,D.M.Belnap
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Key ref:
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J.Lin
et al.
(2013).
Conformational shift of a major poliovirus antigen confirmed by immuno-cryogenic electron microscopy.
J Immunol,
191,
884-891.
PubMed id:
DOI:
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Date:
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10-Apr-13
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Release date:
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03-Jul-13
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Headers
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References
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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P03300
(POLG_POL1M) -
Genome polyprotein from Poliovirus type 1 (strain Mahoney)
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Seq:
Struc:
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2209 a.a.
283 a.a.
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P03300
(POLG_POL1M) -
Genome polyprotein from Poliovirus type 1 (strain Mahoney)
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Seq:
Struc:
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2209 a.a.
268 a.a.
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Enzyme class 2:
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Chains 1, 2, 3, 4:
E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Enzyme class 3:
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Chains 1, 2, 3, 4:
E.C.3.4.22.28
- picornain 3C.
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Reaction:
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Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
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Enzyme class 4:
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Chains 1, 2, 3, 4:
E.C.3.4.22.29
- picornain 2A.
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Reaction:
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Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
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Enzyme class 5:
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Chains 1, 2, 3, 4:
E.C.3.6.1.15
- nucleoside-triphosphate phosphatase.
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Reaction:
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a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
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ribonucleoside 5'-triphosphate
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+
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H2O
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=
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ribonucleoside 5'-diphosphate
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+
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phosphate
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Immunol
191:884-891
(2013)
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PubMed id:
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Conformational shift of a major poliovirus antigen confirmed by immuno-cryogenic electron microscopy.
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J.Lin,
N.Cheng,
J.M.Hogle,
A.C.Steven,
D.M.Belnap.
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ABSTRACT
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Small, interfacial conformational changes occur in some Ag-Ab interactions.
Using cryogenic electron microscopy (cryo-EM), we have demonstrated such changes
in a major antigenic site of a poliovirus capsid protein. During cell entry,
native human poliovirus (160S particle) converts to a cell entry intermediate
(135S particle) and later to an RNA-released (80S) particle. By mixing particles
with Fabs of the neutralizing C3 mAb, we labeled the external loop connecting
the B and C β-strands (BC loop) of the capsid protein VP1 (residues 95-105) in
the 160S and 135S states. We then determined three-dimensional structures by
cryo-EM and enhanced their interpretability by fitting high-resolution
coordinates of C3 Fab and the capsid proteins into the density maps. Binding of
C3 to either 160S or 135S particles caused residues of the BC loop, located on
the tip of a prominent peak known as the "mesa," to move by an
estimated 5 Å. C3 Abs are neutralizing and can bind bivalently. The orientation
of the bound Fabs in our reconstructions suggests that C3 neutralizes poliovirus
by binding two adjacent BC loops on the same mesa and inhibiting conformational
changes in the viral capsid.
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