ArticlePeptides2006
NMR structure of the viral peptide linked to the genome (VPg) of poliovirus.
Article in Peptides, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
- Sequences and Structures of Viral Proteins Linked to the Genomes (VPg) of RNA Viruses.Viruses · 2025Review
- VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.International journal of molecular sciences · 2023Article
- Host Restrictive Factors Are the Emerging Storm Troopers Against Enterovirus: A Mini-Review.Frontiers in immunology · 2022Review
- Protein Nucleotidylylation in +ssRNA Viruses.Viruses · 2021Review
- Functional Characterization of Pepper Vein Banding Virus-Encoded Proteins and Their Interactions: Implications inViruses · 2020Review
- Structural Biology of the Enterovirus Replication-Linked 5'-Cloverleaf RNA and Associated Virus Proteins.Microbiology and molecular biology reviews : MMBR · 2020Review
- Picornaviral polymerase structure, function, and fidelity modulation.Virus research · 2017Review
- Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016Article
- A Conserved Interaction between a C-Terminal Motif in Norovirus VPg and the HEAT-1 Domain of eIF4G Is Essential for Translation Initiation.PLoS pathogens · 2016Article
- Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses.Virology · 2015Article
- Initiation of protein-primed picornavirus RNA synthesis.Virus research · 2015Review
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- Structures of the compact helical core domains of feline calicivirus and murine norovirus VPg proteins.Journal of virology · 2013Article
- Physicochemical property consensus sequences for functional analysis, design of multivalent antigens and targeted antivirals.BMC bioinformatics · 2012Article
- Article
- NMR solution structure of poliovirus uridylyated peptide linked to the genome (VPgpU).Peptides · 2010Article
- Expanding knowledge of P3 proteins in the poliovirus lifecycle.Future microbiology · 2010Review
- Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses.Virology journal · 2009Article
- The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases.Journal of virology · 2008Article
- Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core.Virology · 2008Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
VPgs are essential for replication of picornaviruses, which cause diseases such as poliomyelitis, foot and mouth disease, and the common cold. VPg in infected cells is covalently linked to the 5' end of the viral RNA, or, in a uridylylated form, free in the cytoplasm. We show here the first solution structure for a picornaviral VPg, that of the 22-residue peptide from poliovirus serotype 1. VPg in buffer is inherently flexible, but a single conformer was obtained by adding trimethylamine N-oxide (TMAO). TMAO had only minor effects on the TOCSY spectrum. However, it increased the amount of structured peptide, as indicated by more peaks in the NOESY spectrum and an up to 300% increase in the ratio of normalized NOE cross peak intensities to that in buffer. The data for VPg in TMAO yielded a well defined structure bundle with 0.6 A RMSD (versus 6.6 A in buffer alone), with 10-30 unambiguous constraints per residue. The structure consists of a large loop region from residues 1 to 14, from which the reactive tyrosinate projects outward, and a C-terminal helix from residues 18 to 21 that aligns the sidechains of conserved residues on one face. The structure has a stable docking position at an area on the poliovirus polymerase crystal structure identified as a VPg binding site by mutagenesis studies. Further, UTP and ATP dock in a base-specific manner to the reactive face of VPg, held in place by residues conserved in all picornavirus VPgs.
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Registered trials
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