1MQT

Swine Vesicular Disease Virus coat protein

Summary for 1MQT

• Entry DOI: 10.2210/pdb1mqt/pdb
• Related: 1COV
• Descriptor: Polyprotein, Polyprotein Capsid Protein, OCTANOIC ACID (2-HYDROXY-1-HYDROXYMETHYL-HEPTADEC-3-ENYL)-AMIDE, ... (6 entities in total)
• Functional Keywords: swine vesicular disease virus, svdv coat protein, enterovirus, icosahedral virus, virus
• Biological source: Swine vesicular disease virus; More
• Total number of polymer chains: 4
• Total formula weight: 93725.67

Authors

Verdaguer, N.,Jimenez-Clavero, M.A.,Fita, I.,Ley, V. (deposition date: 2002-09-17, release date: 2004-03-02, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)