1AYM

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

1AYM の概要

• エントリーDOI: 10.2210/pdb1aym/pdb
• 分子名称: HUMAN RHINOVIRUS 16 COAT PROTEIN, ZINC ION, LAURIC ACID, ... (8 entities in total)
• 機能のキーワード: human rhinovirus 16, rna, site-directed mutagenesis, rhinovirus coat protein, icosahedral virus, virus
• 由来する生物種: Human rhinovirus sp.; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95674.28

構造登録者

Hadfield, A.T.,Rossmann, M.G. (登録日: 1997-11-06, 公開日: 1998-01-21, 最終更新日: 2024-12-25)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)