Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design.
Grant, R.A., Hiremath, C.N., Filman, D.J., Syed, R., Andries, K., Hogle, J.M.(1994) Curr Biol 4: 784-797
- PubMed: 7820548 
- DOI: https://doi.org/10.1016/s0960-9822(00)00176-7
- Primary Citation of Related Structures:  
1VBA, 1VBB, 1VBC, 1VBD, 1VBE - 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.
Organizational Affiliation: 
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.