Literature summary for 3.4.21.98 extracted from

Romano, K.P.; Laine, J.M.; Deveau, L.M.; Cao, H.; Massi, F.; Schiffer, C.A.
Molecular mechanisms of viral and host cell substrate recognition by hepatitis C virus NS3/4A protease (2011), J. Virol., 85, 6106-6116.

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Cloned(Commentary)

Cloned (Comment)	Organism
expresssed in Escherichia coli	Hepacivirus C

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Hepacivirus C	-	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
NS3/4A protease	-	Hepacivirus C