1PO2

POLIOVIRUS (TYPE 1, MAHONEY) IN COMPLEX WITH R77975, AN INHIBITOR OF VIRAL REPLICATION

Summary for 1PO2

• Entry DOI: 10.2210/pdb1po2/pdb
• Descriptor: POLIOVIRUS TYPE 1 MAHONEY, (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE, MYRISTIC ACID, ... (7 entities in total)
• Functional Keywords: poliovirus, picornavirus coat protein, anti-viral drugs, hydrolase, thiol protease, icosahedral virus, virus
• Biological source: Human poliovirus 1; More
• Cellular location: Capsid protein VP0: Virion. Capsid protein VP4: Virion. Capsid protein VP2: Virion. Capsid protein VP3: Virion. Capsid protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion. Protease 3C: Host cytoplasm. Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P03300 P03300 P03300
• Total number of polymer chains: 5
• Total formula weight: 98540.16

Authors

Hiremath, C.N.,Filman, D.J.,Grant, R.A.,Hogle, J.M. (deposition date: 1997-01-08, release date: 1997-12-03, Last modification date: 2023-08-09)

Primary citation

Hiremath, C.N.,Filman, D.J.,Grant, R.A.,Hogle, J.M.
Ligand-induced conformational changes in poliovirus-antiviral drug complexes.
Acta Crystallogr.,Sect.D, 53:558-570, 1997

PubMed Abstract: 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.

PubMed: 15299887
DOI: 10.1107/S0907444997000954

Experimental method

X-RAY DIFFRACTION (2.9 Å)