Crystal Structure of a Novel Conformational State of the Flavivirus NS3 Protein: Implications for Polyprotein Processing and Viral Replication (Q27490476)

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English	Crystal Structure of a Novel Conformational State of the Flavivirus NS3 Protein: Implications for Polyprotein Processing and Viral Replication	scientific article

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scholarly article

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8 February 2020

Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication (English)

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8 February 2020

viral genome replication

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based on heuristic

inferred from abstract

crystal structure

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protein structure

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1 reference

structural biology

1 reference

dengue virus protein NS3

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based on heuristic

inferred from abstract

5

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8 February 2020

Eloise Mastrangelo

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8 February 2020

Thomas S. Walter

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8 February 2020

David Ian Stuart

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8 February 2020

Erika J Mancini

9

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8 February 2020

Jonathan Grimes

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object named as

Jonathan M Grimes

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8 February 2020

author name string

René Assenberg

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8 February 2020

Anil Verma

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publication date

30 September 2009

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8 February 2020

Journal of Virology

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8 February 2020

83

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8 February 2020

12895-12906

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8 February 2020

24

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8 February 2020

describes a project that uses

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Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation

1 reference

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Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein

1 reference

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Recognition of RNA cap in the Wesselsbron virus NS5 methyltransferase domain: implications for RNA-capping mechanisms in Flavivirus

1 reference

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Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis

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Yellow Fever Virus NS3 Plays an Essential Role in Virus Assembly Independent of Its Known Enzymatic Functions

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Crystal Structure of the NS3 Protease-Helicase from Dengue Virus

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1 reference

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1 reference

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1 reference

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Structure of the Dengue Virus Helicase/Nucleoside Triphosphatase Catalytic Domain at a Resolution of 2.4 A

1 reference

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20 March 2017

Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing

1 reference

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An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization

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Paired charge-to-alanine mutagenesis of dengue virus type 4 NS5 generates mutants with temperature-sensitive, host range, and mouse attenuation phenotypes

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Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase

1 reference

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The serine protease and RNA-stimulated nucleoside triphosphatase and RNA helicase functional domains of dengue virus type 2 NS3 converge within a region of 20 amino acids

1 reference

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1 reference

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Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes

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Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins

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The CCP4 suite: programs for protein crystallography

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PHENIX: building new software for automated crystallographic structure determination

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Main-chain bond lengths and bond angles in protein structures

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Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity

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Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.

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Modulation of the nucleoside triphosphatase/RNA helicase and 5'-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase.

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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27 November 2018

Identifiers

10.1128/JVI.00942-09

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8 February 2020

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Europe PubMed Central

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8 February 2020

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8 February 2020

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