1ayn
From Proteopedia
|
HUMAN RHINOVIRUS 16 COAT PROTEIN
Overview
BACKGROUND: 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. RESULTS: We have determined the structure of HRV16, another ... [(full description)]
About this Structure
1AYN is a [Protein complex] structure of sequences from [Human rhinovirus sp.] with ZN, DAO and MYR as [ligands]. This structure superseeds the now removed PDB entry 2RHN. Full crystallographic information is available from [OCA].
Reference
The structure of human rhinovirus 16., Oliveira MA, Zhao R, Lee WM, Kremer MJ, Minor I, Rueckert RR, Diana GD, Pevear DC, Dutko FJ, McKinlay MA, et al., Structure. 1993 Sep 15;1(1):51-68. PMID:7915182
Page seeded by OCA on Mon Oct 29 22:13:08 2007
