Literature summary for 3.4.21.113 extracted from

Beran, R.K.; Serebrov, V.; Pyle, A.M.
The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate (2007), J. Biol. Chem., 282, 34913-34920.

Search for more literature for 3.4.21.113

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	protease domain of the NS3 protein greatly enhances both the direct and functional binding of RNA to NS3. Electrostatics play an important role in this process, protease domain is the most positively charged region of the NS3 protein and it provides an electrostatic potential that exceeds even that of the positively charged ATPase site on the protein. Protease domain is required for RNA unwinding by NS3	Hepacivirus C

Application

Application	Comment	Organism
medicine	NS3 protease domain is essential for the process of viral RNA replication and, given its electrostatic contribution to RNA binding, it may also assist in packaging of the viral RNA	Hepacivirus C

Cloned(Commentary)

Cloned (Comment)	Organism
into vectors pET15b and pET-SUMO	Hepacivirus C

Protein Variants

Protein Variants	Comment	Organism
additional information	protease deletion constructs of the helicase domain NS3hel(deltaN166) and NS3hel(deltaN188), which are missing 166 and 188 amino acids, respectively, from the N-terminus of the NS3 protein. NS3hel(deltaN188) binds TS34 RNA, RNA binding by NS3hel(deltaN166) is not detectable	Hepacivirus C

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	specific allosteric contribution from the interaction interface between NS3 helicase and the protease domain	Hepacivirus C

Organism

Organism	UniProt	Comment	Textmining
Hepacivirus C	-	genotype 1a, version H77	-

Purification (Commentary)

Purification (Comment)	Organism
on nickel column and by gel filtration	Hepacivirus C

Synonyms

Synonyms	Comment	Organism
nonstructural protein 3	-	Hepacivirus C
NS3 protein	-	Hepacivirus C

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Release 2023.1 (January 2023)