Cloned (Comment) | Organism |
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expresssed in Escherichia coli | Hepacivirus C |
Crystallization (Comment) | Organism |
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NS3/4A crystal structures of both host cell cleavage sites are determined and compared to the crystal structures of viral substrates. Two distinct protease conformations are observed and correlate with substrate specificity: 3-4A, 4A4B, 5A5B, and MAVS, which are processed more efficiently by the protease, form extensive electrostatic networks when in complex with the protease, and TRIF and 4B5A, which contain polyproline motifs in their full-length sequences, do not form electrostatic networks in their crystal complexes | Hepacivirus C |
Protein Variants | Comment | Organism |
---|---|---|
S139A | this NS3/4A construct contains the inactivating mutation S139A, which is designed to further enhance protein stability by minimizing autoproteolysis during the crystallization process | Hepacivirus C |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
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additional information | Hepacivirus C | NS3/4A protease is responsible for cleaving the viral polyprotein at junctions 3-4A, 4A4B, 4B5A, and 5A5B and two host cell adaptor proteins of the innate immune response, TRIF and MAVS | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Hepacivirus C | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | NS3/4A protease is responsible for cleaving the viral polyprotein at junctions 3-4A, 4A4B, 4B5A, and 5A5B and two host cell adaptor proteins of the innate immune response, TRIF and MAVS | Hepacivirus C | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NS3/4A protease | - |
Hepacivirus C |