Literature summary for 3.4.21.91 extracted from

Aguilera-Pesantes, D.; Robayo, L.E.; Mendez, P.E.; Mollocana, D.; Marrero-Ponce, Y.; Torres, F.J.; Mendez, M.A.
Discovering key residues of dengue virus NS2b-NS3-protease new binding sites for antiviral inhibitors design (2017), Biochem. Biophys. Res. Commun., 492, 631-642 .

Search for more literature for 3.4.21.91

Application

Application	Comment	Organism
drug development	the essential enzyme is a target for drug design	Dengue virus type 3

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	structure-based identification of key residues and binding sites for inhibitor binding, design of non-competitive inhibitors for Dengue virus type 3 NS2b-NS3-protease, overview. The identified residues include 1. amino acids close to the beta sheet-loop-beta sheet known to be important in its closed conformation for NS2b 2. residues close to the active site, 3. several residues evenly spread on the NS2b-NS3 contact surface, and 4. some inner residues most likely related to the overall stability of the protease. Computational alanine scanning mutagenesis and similarity analysis based on sequence and structure homology, modeling. On the DENV NS3 protease, the residues Tyr23, Gly37, Phe46, Thr48, His51, Thr53, Leu58, Asp75, Tyr79, Trp89, and Thr156 are identified as class A and as the eleven highest ranked residues by both MLP models	Dengue virus type 3

Organism

Organism	UniProt	Comment	Textmining
Dengue virus type 3	Q5UB51	DENV-3	-
Dengue virus type 3 Singapore/8120/1995	Q5UB51	DENV-3	-

Synonyms

Synonyms	Comment	Organism
Dengue NS2b-NS3 protease	-	Dengue virus type 3
NS2b-NS3-protease	-	Dengue virus type 3

Cofactor

Cofactor	Comment	Organism	Structure
NS2B cofactor	-	Dengue virus type 3

General Information

General Information	Comment	Organism
physiological function	the NS2B-NS3 protease is essential for the dengue virus (DENV) replication process	Dengue virus type 3

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Release 2023.1 (January 2023)