Solution structure and dynamics of the single-chain hepatitis C virus NS3 rotease NS4A cofactor complex

Journal of Molecular Biology

Volumn 305, Issue 5, 2001, Pages 1099-1110

  McCoy, Mark A ^a   Senior, Mary M ^a   Gesell, Jennifer J ^a   Ramanathan, Lata ^a   Wyss, Daniel F ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

Dynamics; HCV; NMR; NS3; Protease

Indexed keywords

PROTEINASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CRYSTALLIZATION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; HEPATITIS C VIRUS; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL;

HEPATITIS C VIRUS;

EID: 0035793211     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4365     Document Type: Article

References (42)

1. Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA
2. An assay for circulating antibodies to a major etiologic virus of human non-A, non-B hepatitis
3. The scientific challenge of hepatitis
4. Variability of hepatitis C virus genome
5. Review: Molecular biology of the hepatitis C virus
6. Treatment strategies for chronic hepatitis C: Update since the 1997 National Institutes of Health Consensus Development Conference
7. Hepatitis C viruses
8. Molecular virology of hepatitis C virus: An update with respect to potential antiviral targets
9. The nonstructural proteins of the hepatitis C virus: Structure and functions
10. Molecular cloning of the human hepatitis C virus genome from Japanese patients with non-A, non-B hepatitis
11. Structure and organization of the hepatitis C virus genome isolated from human carriers
12. Expression and identification of hepatitis C virus polyprotein cleavage products
13. Complex processing and protein:protein interactions in the E2:NS2 region of HCV
14. A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro
15. Non-structural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
16. Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites
17. Expression, isolation, and characterization of the hepatitis C virus ATPase/RNA helicase
18. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity
19. Kinetic and structural analyses of hepatitis C virus polyprotein processing
20. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus non-structural proteins
21. Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini
22. Hepatitis C virus NS3 serine proteinase: Trans-cleavage requirements and processing kinetics
23. Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing
24. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc-binding site
25. The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism
26. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
27. Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 Å resolution structure in a hexagonal crystal form
28. Molecular views of viral poly-protein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
29. Mechanistic role of an NS4A peptide cofactor with the truncated NS3 protease of hepatitis C virus: Elucidation of the NS4A stimulatory effect via kinetic analysis and inhibitor mapping
30. Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain
31. Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease
32. Complex formation between the hepatitis C virus serine protease and a synthetic NS4A cofactor peptide
33. Conformational changes in human hepatitis C virus NS3 protease upon binding of product-based inhibitors
34. 13C chemical-shift data
35. A model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
36. A model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
37. Discovering high-affinity ligands for proteins: SAR by NMR
38. Solution structures of stromelysin complexed to thiadiazole inhibitors
39. Methodological advances in protein NMR
40. Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
41. Molscript: A program to produce both detailed and schematic plots of protein structures
42. Grasp: Graphical representation and analysis of surface properties