1AYM

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

Summary for 1AYM

• Entry DOI: 10.2210/pdb1aym/pdb
• Descriptor: HUMAN RHINOVIRUS 16 COAT PROTEIN, ZINC ION, LAURIC ACID, ... (8 entities in total)
• Functional Keywords: human rhinovirus 16, rna, site-directed mutagenesis, 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.,Rossmann, M.G. (deposition date: 1997-11-06, release date: 1998-01-21, Last modification date: 2024-12-25)

Primary citation

Hadfield, A.T.,Lee, W.,Zhao, R.,Oliveira, M.A.,Minor, I.,Rueckert, R.R.,Rossmann, M.G.
The refined structure of human rhinovirus 16 at 2.15 A resolution: implications for the viral life cycle.
Structure, 5:427-441, 1997

PubMed Abstract: Rhinoviruses belong to the picornavirus family and are small, icosahedral, non-enveloped viruses containing one positive RNA strand. Human rhinovirus 16 (HRV16) belongs to the major receptor group of rhinoviruses, for which the cellular receptor is intercellular adhesion molecule-1 (ICAM-1). In many rhinoviruses, one of the viral coat proteins (VP1) contains a hydrophobic pocket which is occupied by a fatty acid-like molecule, or so-called 'pocket factor'. Antiviral agents have been shown to bind to the hydrophobic pocket in VP1, replacing the pocket factor. The presence of the antiviral compound blocks uncoating of the virus and in some cases inhibits receptor attachment. A refined, high-resolution structure would be expected to provide further information on the nature of the pocket factor and other features previously not clearly identified.

PubMed: 9083115
DOI: 10.1016/S0969-2126(97)00199-8

Experimental method

X-RAY DIFFRACTION (2.15 Å)