ArticleBiochemistry2012
Dengue virus nonstructural protein 5 adopts multiple conformations in solution.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
- Solanaceae-Derived Spirostane Saponins Inhibit Dengue Virus Replication and Viral Protein Expression and Exhibit Activity Against Multiple Arboviruses.Drug development research · 2026Article
- Article
- Phosphorylation landscape of dengue virus proteins and their implications in protein-protein interactions.PloS one · 2026Article
- Structural dynamics of the dengue virus non-structural 5 (NS5) interactions with promoter stem-loop A (SLA).Npj viruses · 2025Article
- A conformational selection mechanism of flavivirus NS5 for species-specific STAT2 inhibition.Communications biology · 2024Article
- Structural basis for cloverleaf RNA-initiated viral genome replication.Nucleic acids research · 2023Article
- Advances in Computational Methods to Discover New NS2B-NS3 Inhibitors Useful Against Dengue and Zika Viruses.Current topics in medicinal chemistry · 2022Review
- Identification of the viral RNA promoter stem loop A (SLA)-binding site on Zika virus polymerase NS5.Scientific reports · 2020Article
- A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase.PLoS pathogens · 2020Article
- Exploring Evolutionary Constraints in the Proteomes of Zika, Dengue, and Other Flaviviruses to Find Fitness-Critical Sites.Journal of molecular evolution · 2020Article
- NS5 from Dengue Virus Serotype 2 Can Adopt a Conformation Analogous to That of Its Zika Virus and Japanese Encephalitis Virus Homologues.Journal of virology · 2019Article
- Suppression of Type I Interferon Signaling byViruses · 2018Review
- Structure and function of Zika virus NS5 protein: perspectives for drug design.Cellular and molecular life sciences : CMLS · 2018Review
- Organization of the Flavivirus RNA replicase complex.Wiley interdisciplinary reviews. RNA · 2017Review
- Interactions between the Dengue Virus Polymerase NS5 and Stem-Loop A.Journal of virology · 2017Article
- The structure of Zika virus NS5 reveals a conserved domain conformation.Nature communications · 2017Article
- A novel indirect ELISA for diagnosis of dengue fever.The Indian journal of medical research · 2016Article
- Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016Article
- Dengue Virus Nonstructural Protein 5 (NS5) Assembles into a Dimer with a Unique Methyltransferase and Polymerase Interface.PLoS pathogens · 2016Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dengue virus (DENV) nonstructural protein 5 (NS5) is composed of two globular domains separated by a 10-residue linker. The N-terminal domain participates in the synthesis of a mRNA cap 1 structure ((7Me)GpppA(2'OMe)) at the 5' end of the viral genome and possesses guanylyltransferase, guanine-N7-methyltransferase, and nucleoside-2'O-methyltransferase activities. The C-terminal domain is an RNA-dependent RNA polymerase responsible for viral RNA synthesis. Although crystal structures of the two isolated domains have been obtained, there are no structural data for full-length NS5. It is also unclear whether the two NS5 domains interact with each other to form a stable structure in which the relative orientation of the two domains is fixed. To investigate the structure and dynamics of DENV type 3 NS5 in solution, we conducted small-angle X-ray scattering experiments with the full-length protein. NS5 was found to be monomeric and well-folded under the conditions tested. The results of these experiments also suggest that NS5 adopts multiple conformations in solution, ranging from compact to more extended forms in which the two domains do not seem to interact with each other. We interpret the multiple conformations of NS5 observed in solution as resulting from weak interactions between the two NS5 domains and flexibility of the linker in the absence of other components of the replication complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.