1VBD
POLIOVIRUS (TYPE 1, MAHONEY STRAIN) COMPLEXED WITH R78206
Summary for 1VBD
Entry DOI | 10.2210/pdb1vbd/pdb |
Descriptor | POLIOVIRUS TYPE 1 MAHONEY, (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE, MYRISTIC ACID, ... (7 entities in total) |
Functional Keywords | virus coat protein, 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 | 98554.19 |
Authors | Grant, R.A.,Hiremath, C.N.,Filman, D.J.,Syed, R.,Andries, K.,Hogle, J.M. (deposition date: 1996-01-02, release date: 1996-07-11, Last modification date: 2023-04-19) |
Primary citation | Grant, R.A.,Hiremath, C.N.,Filman, D.J.,Syed, R.,Andries, K.,Hogle, J.M. Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design. Curr.Biol., 4:784-797, 1994 Cited by PubMed Abstract: Picornaviruses, such as the structurally related polioviruses and rhinoviruses, are important human pathogens which have been the target of major drug development efforts. Receptor-mediated uncoating and thermal inactivation of poliovirus and rhinovirus are inhibited by agents that bind to each virus by inserting into a pocket in the beta barrel of the viral capsid protein, VP1. This pocket, which is normally empty in human rhinovirus-14 (HRV14), is occupied by an unknown natural ligand in poliovirus. Structural studies of HRV14-drug complexes have shown that drug binding causes large, localized changes in the conformation of VP1. PubMed: 7820548DOI: 10.1016/S0960-9822(00)00176-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report