1PO2

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

1PO2 の概要

• エントリーDOI: 10.2210/pdb1po2/pdb
• 分子名称: POLIOVIRUS TYPE 1 MAHONEY, (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE, MYRISTIC ACID, ... (7 entities in total)
• 機能のキーワード: poliovirus, picornavirus coat protein, anti-viral drugs, hydrolase, thiol protease, icosahedral virus, virus
• 由来する生物種: Human poliovirus 1; 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 98540.16

構造登録者

Hiremath, C.N.,Filman, D.J.,Grant, R.A.,Hogle, J.M. (登録日: 1997-01-08, 公開日: 1997-12-03, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)