Summary for 1AYN
| Entry DOI | 10.2210/pdb1ayn/pdb |
| Descriptor | HUMAN RHINOVIRUS 16 COAT PROTEIN, ZINC ION, LAURIC ACID, ... (8 entities in total) |
| Functional Keywords | human rhinovirus 16, receptor, drug, rhinovirus coat protein, icosahedral virus, virus |
| Biological source | Human rhinovirus sp. More |
| Total number of polymer chains | 4 |
| Total formula weight | 95674.28 |
| Authors | Hadfield, A.T.,Oliveira, M.A.,Zhao, R.,Rossmann, M.G. (deposition date: 1997-11-06, release date: 1998-01-21, Last modification date: 2023-08-09) |
| Primary citation | 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. The structure of human rhinovirus 16. Structure, 1:51-68, 1993 Cited by 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. PubMed: 7915182DOI: 10.1016/0969-2126(93)90008-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
