1MQT

Swine Vesicular Disease Virus coat protein

1MQT の概要

• エントリーDOI: 10.2210/pdb1mqt/pdb
• 関連するPDBエントリー: 1COV
• 分子名称: Polyprotein, Polyprotein Capsid Protein, OCTANOIC ACID (2-HYDROXY-1-HYDROXYMETHYL-HEPTADEC-3-ENYL)-AMIDE, ... (6 entities in total)
• 機能のキーワード: swine vesicular disease virus, svdv coat protein, enterovirus, icosahedral virus, virus
• 由来する生物種: Swine vesicular disease virus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93725.67

構造登録者

Verdaguer, N.,Jimenez-Clavero, M.A.,Fita, I.,Ley, V. (登録日: 2002-09-17, 公開日: 2004-03-02, 最終更新日: 2024-02-14)

主引用文献

Verdaguer, N.,Jimenez-Clavero, M.A.,Fita, I.,Ley, V.
STRUCTURE OF SWINE VESICULAR DISEASE VIRUS: MAPPING OF CHANGES OCCURRING DURING ADAPTATION OF HUMAN COXSACKIE B5 VIRUS TO INFECT SWINE
J.Virol., 77:9780-9789, 2003

PubMed Abstract: The structure of swine vesicular disease virus (SVDV) was solved and refined at a 3.0-A resolution by X-ray crystallography to gain information about the role of sequence changes that occurred as this virus evolved from the parental human pathogen coxsackievirus B5 (CVB5). These amino acid substitutions can be clustered in five distinct regions: (i) the antigenic sites, (ii) the hydrophobic pocket of the VP1 beta-sandwich, (iii) the putative CAR binding site, (iv) the putative heparan sulfate binding site, and (v) the fivefold axis. The VP1 pocket is occupied by a branched pocket factor, apparently different from that present in the closely related virus CVB3 and in other picornaviruses. This finding may be relevant for the design of new antiviral compounds against this site. Density consistent with the presence of ions was observed on the fivefold and threefold axes. The structure also provided an accurate description of the putative receptor binding sites.

PubMed: 12941886
DOI: 10.1128/JVI.77.18.9780-9789.2003

実験手法

X-RAY DIFFRACTION (3.3 Å)