The structure of human rhinovirus 16.
Oliveira, M.A., Zhao, R., Lee, W.M., Kremer, M.J., Minor, I., Rueckert, R.R., Diana, G.D., Pevear, D.C., Dutko, F.J., McKinlay, M.A., Rossmann, M.G.(1993) Structure 1: 51-68
- PubMed: 7915182 
- DOI: https://doi.org/10.1016/0969-2126(93)90008-5
- Primary Citation of Related Structures:  
1AYN - PubMed Abstract: 
Rhinoviruses and the homologous polioviruses have hydrophobic pockets below their receptor-binding sites, which often contain unidentified electron density ('pocket factors'). Certain antiviral compounds also bind in the pocket, displacing the pocket factor and inhibiting uncoating. However, human rhinovirus (HRV)14, which belongs to the major group of rhinoviruses that use intercellular adhesion molecule-1 (ICAM-1) as a receptor, has an empty pocket. When antiviral compounds bind into the empty pocket of HRV14, the roof of the pocket, which is also the floor of the receptor binding site (the canyon), is deformed, preventing receptor attachment. The role of the pocket in viral infectivity is not known.
Organizational Affiliation: 
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.