1VBA

POLIOVIRUS (TYPE 3, SABIN STRAIN) (P3/SABIN, P3/LEON/12A(1)B) COMPLEXED WITH R78206

Summary for 1VBA

• Entry DOI: 10.2210/pdb1vba/pdb
• Descriptor: POLIOVIRUS TYPE 3, (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE, MYRISTIC ACID, ... (7 entities in total)
• Functional Keywords: virus coat protein, hydrolase, thiol protease, icosahedral virus, virus
• Biological source: Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B); More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P03302 P03302 P03302 P03302
• Total number of polymer chains: 5
• Total formula weight: 98023.58

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: 2024-10-23)

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

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: 7820548
DOI: 10.1016/S0960-9822(00)00176-7

Experimental method

X-RAY DIFFRACTION (2.9 Å)