Pasquo et al., 1998 - Google Patents
Rational design and functional expression of a constitutively active single-chain NS4A–NS3 proteinasePasquo et al., 1998
View HTML- Document ID
- 298565689486560765
- Author
- Pasquo A
- Nardi M
- Dimasi N
- Tomei L
- Steinkühler C
- Delmastro P
- Tramontano A
- De Francesco R
- Publication year
- Publication venue
- Folding and Design
External Links
Snippet
Background: The proteinase domain of the hepatitis C virus NS3 protein is involved in the maturation of the viral polyprotein. A central hydrophobic domain of the NS4A protein is required as a cofactor for its proteolytic activity. The three-dimensional structure of the …
- 102000035443 Peptidases 0 title abstract description 137
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/503—Proteinases Endopeptidases (3.4.21-3.4.25) derived from viruses
- C12N9/506—Proteinases Endopeptidases (3.4.21-3.4.25) derived from viruses derived from RNA viruses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2770/00—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA Viruses positive-sense
- C12N2770/00011—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA Viruses positive-sense ssRNA Viruses positive-sense
- C12N2770/24011—Flaviviridae
- C12N2770/24211—Hepacivirus, e.g. hepatitis C virus, hepatitis G virus
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
- G01N33/576—Immunoassay; Biospecific binding assay for hepatitis
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Kim et al. | Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide | |
Yao et al. | Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase | |
Love et al. | The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site | |
Bera et al. | Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease | |
Lorenz et al. | Structure of the catalytic domain of the hepatitis C virus NS2-3 protease | |
Reid et al. | Chromophore formation in green fluorescent protein | |
Wu et al. | Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing | |
Sweeney et al. | Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the β-ribbon in proteolysis | |
Gallinari et al. | Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus | |
Kim et al. | Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding | |
Frick et al. | The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently | |
Ferreon et al. | Molecular determinants of TRIF proteolysis mediated by the hepatitis C virus NS3/4A protease | |
Zou et al. | Mapping the interactions between the NS4B and NS3 proteins of dengue virus | |
Li et al. | Functional profiling of recombinant NS3 proteases from all four serotypes of dengue virus using tetrapeptide and octapeptide substrate libraries | |
Pallaoro et al. | Characterization of the hepatitis C virus NS2/3 processing reaction by using a purified precursor protein | |
Belliot et al. | In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells | |
Sali et al. | Serine protease of hepatitis C virus expressed in insect cells as the NS3/4A complex | |
Chuck et al. | Profiling of substrate specificity of SARS-CoV 3CLpro | |
Gallinari et al. | Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A | |
Choksupmanee et al. | Structural platform for the autolytic activity of an intact NS2B–NS3 protease complex from dengue virus | |
Shannon et al. | Simultaneous uncoupled expression and purification of the Dengue virus NS3 protease and NS2B co-factor domain | |
Wu et al. | Activation of dengue protease autocleavage at the NS2B–NS3 junction by recombinant NS3 and GST–NS2B fusion proteins | |
Martin et al. | Design of selective eglin inhibitors of HCV NS3 proteinase | |
Failla et al. | Redesigning the substrate specificity of the hepatitis C virus NS3 protease | |
US6333186B1 (en) | Modified forms of Hepatitis C NS3 protease for facilitating inhibitor screening and structural studies of protease: inhibitor complexes |