1po2
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| , resolution 2.9Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
POLIOVIRUS (TYPE 1, MAHONEY) IN COMPLEX WITH R77975, AN INHIBITOR OF VIRAL REPLICATION
OverviewOverview
Crystal structures of the Mahoney strain of type 1 poliovirus complexed with the antiviral compounds R80633 and R77975 were determined at 2.9 A resolution. These compounds block infection by preventing conformational changes required for viral uncoating. In various drug-poliovirus complexes reported earlier, no significant conformational changes were found in the structures of the capsid proteins. In the structures reported here, the strain of virus is relatively insensitive to these antivirals. Correspondingly, significant conformational changes are necessary to accommodate the drug. These conformational changes affect both the immediate vicinity of the drug binding site, and more distant loops located near the fivefold axis. In addition, small but concerted shifts of the centers of mass of the major capsid proteins consistently have been detected whose magnitudes are correlated inversely with the effectiveness of the drugs. Collectively, the drug complexes appear to sample the conformational repertoire of poliovirus near equilibrium, and thus provide a possible model for the earliest stages of viral uncoating during infection.
About this StructureAbout this Structure
1PO2 is a Protein complex structure of sequences from Human poliovirus 1. Full crystallographic information is available from OCA.
ReferenceReference
Ligand-induced conformational changes in poliovirus-antiviral drug complexes., Hiremath CN, Filman DJ, Grant RA, Hogle JM, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):558-70. PMID:15299887
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