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PDBsum entry 1xr5
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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 crystal structure of the RNA-Dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy.
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Authors
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R.A.Love,
K.A.Maegley,
X.Yu,
R.A.Ferre,
L.K.Lingardo,
W.Diehl,
H.E.Parge,
P.S.Dragovich,
S.A.Fuhrman.
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Ref.
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Structure, 2004,
12,
1533-1544.
[DOI no: ]
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PubMed id
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Abstract
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Human rhinoviruses (HRV), the predominant members of the Picornaviridae family
of positive-strand RNA viruses, are the major causative agents of the common
cold. Given the lack of effective treatments for rhinoviral infections, virally
encoded proteins have become attractive therapeutic targets. The HRV genome
encodes an RNA-dependent RNA polymerase (RdRp) denoted 3Dpol, which is
responsible for replicating the viral genome and for synthesizing a protein
primer used in the replication. Here the crystal structures for three viral
serotypes (1B, 14, and 16) of HRV 3Dpol have been determined. The three
structures are very similar to one another, and to the closely related
poliovirus (PV) 3Dpol enzyme. Because the reported PV crystal structure shows
significant disorder, HRV 3Dpol provides the first complete view of a
picornaviral RdRp. The folding topology of HRV 3Dpol also resembles that of
RdRps from hepatitis C virus (HCV) and rabbit hemorrhagic disease virus (RHDV)
despite very low sequence homology.
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Figure 1.
Figure 1. Experimental Density Map for HRV 3D^polStereoview
of the 2.8 Å SAD electron density map for HRV14 3D^pol in the
vicinity of the active site (contoured at 2s), derived from
SHARP using the anomalous signal of bound samarium (red sphere).
The refined structure of HRV14 3D^pol is superimposed.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
1533-1544)
copyright 2004.
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