Literature summary for 3.4.21.98 extracted from

Meeprasert, A.; Hannongbua, S.; Rungrotmongkol, T.
Key binding and susceptibility of NS3/4A serine protease inhibitors against hepatitis C virus (2014), J. Chem. Inf. Model., 54, 1208-1217.

Search for more literature for 3.4.21.98

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations using inhibitors boceprevir, telaprevir, danoprevir, and BI201335. The key residues involved in inhibitor binding are residues 41-43, 57, 81, 136-139, 155-159, and 168 in the NS3 domain. The van der Waals interactions yield the main driving force for inhibitor binding at the protease active site for the cleavage reaction. In addition, the highest number of hydrogen bonds is formed at the reactive P1 site of the four studied inhibitors.The P3 site is most likely to be recognized by the A157 backbone. The relative binding affinities predicted for the four inhibitors are in a somewhat similar trend to their experimentally derived biological activities	Hepacivirus C

Crystallization (Comment)

Organism

molecular dynamics simulations using inhibitors boceprevir, telaprevir, danoprevir, and BI201335. The key residues involved in inhibitor binding are residues 41-43, 57, 81, 136-139, 155-159, and 168 in the NS3 domain. The van der Waals interactions yield the main driving force for inhibitor binding at the protease active site for the cleavage reaction. In addition, the highest number of hydrogen bonds is formed at the reactive P1 site of the four studied inhibitors.The P3 site is most likely to be recognized by the A157 backbone. The relative binding affinities predicted for the four inhibitors are in a somewhat similar trend to their experimentally derived biological activities

Hepacivirus C

Inhibitors

Inhibitors	Comment	Organism
BI201335	-	Hepacivirus C
boceprevir	-	Hepacivirus C
danoprevir	-	Hepacivirus C
telaprevir	-	Hepacivirus C

Organism

Organism	UniProt	Comment	Textmining
Hepacivirus C	-	-	-

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Release 2023.1 (January 2023)