ArticleActa crystallographica. Section D, Biological crystallography2015
Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- Dengue Virus NS5 Target Discovery: A Comprehensive in Silico Exploration of Novel Druggable Sites for Pan-Serotype Antiviral Design.International journal of molecular sciences · 2026Article
- Structural dynamics of the dengue virus non-structural 5 (NS5) interactions with promoter stem-loop A (SLA).Npj viruses · 2025Article
- Galidesivir Triphosphate Promotes Stalling of Dengue-2 Virus Polymerase Immediately Prior to Incorporation.ACS infectious diseases · 2023Article
- Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity.Nucleic acids research · 2022Article
- A conserved arginine in NS5 binds genomic 3' stem-loop RNA for primer-independent initiation of flavivirus RNA replication.RNA (New York, N.Y.) · 2022Article
- Virtual Screening of Drug-Like Compounds as Potential Inhibitors of the Dengue Virus NS5 Protein.Frontiers in chemistry · 2022Article
- Review
- Article
- A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase.PLoS pathogens · 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
- Supramolecular arrangement of the full-length Zika virus NS5.PLoS pathogens · 2019Article
- Pyrazinoic Acid Inhibits Mycobacterial Coenzyme A Biosynthesis by Binding to Aspartate Decarboxylase PanD.ACS infectious diseases · 2017Article
- Combining NMR and small angle X-ray scattering for the study of biomolecular structure and dynamics.Archives of biochemistry and biophysics · 2017Review
- Interactions between the Dengue Virus Polymerase NS5 and Stem-Loop A.Journal of virology · 2017Article
- Structural features of NS3 of Dengue virus serotypes 2 and 4 in solution and insight into RNA binding and the inhibitory role of quercetin.Acta crystallographica. Section D, Structural biology · 2017Article
- Dengue Virus Non-Structural Protein 5.Viruses · 2017Review
- Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.The Journal of biological chemistry · 2017Article
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Infection by the four serotypes of Dengue virus (DENV-1 to DENV-4) causes an important arthropod-borne viral disease in humans. The multifunctional DENV nonstructural protein 5 (NS5) is essential for capping and replication of the viral RNA and harbours a methyltransferase (MTase) domain and an RNA-dependent RNA polymerase (RdRp) domain. In this study, insights into the overall structure and flexibility of the entire NS5 of all four Dengue virus serotypes in solution are presented for the first time. The solution models derived revealed an arrangement of the full-length NS5 (NS5FL) proteins with the MTase domain positioned at the top of the RdRP domain. The DENV-1 to DENV-4 NS5 forms are elongated and flexible in solution, with DENV-4 NS5 being more compact relative to NS5 from DENV-1, DENV-2 and DENV-3. Solution studies of the individual MTase and RdRp domains show the compactness of the RdRp domain as well as the contribution of the MTase domain and the ten-residue linker region to the flexibility of the entire NS5. Swapping the ten-residue linker between DENV-4 NS5FL and DENV-3 NS5FL demonstrated its importance in MTase-RdRp communication and in concerted interaction with viral and host proteins, as probed by amide hydrogen/deuterium mass spectrometry. Conformational alterations owing to RNA binding are presented.
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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.