Literature summary for 3.4.21.91 extracted from

Luo, D.; Wei, N.; Doan, D.N.; Paradkar, P.N.; Chong, Y.; Davidson, A.D.; Kotaka, M.; Lescar, J.; Vasudevan, S.G.
Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications (2010), J. Biol. Chem., 285, 18817-18827.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the identification of an alternative stable conformation for the full-length NS2B18NS3 protein is reported. In this second conformation refined to a resolution of 2.2 A, the protease domain has rotated by an angle of 161° relative to the helicase domain	Dengue virus type 4

Protein Variants

Protein Variants	Comment	Organism
additional information	mutation in the 11-amino acid linker region (169-179): a Gly residue before Pro174 is introduced in DENV4 NS2B18NS3: The mutant protein having a glycine insertion in its linker region adopts another conformation where the protease domain has not rotated by an angle of 161° relative to the helicase domain	Dengue virus type 4
P176G	mutation in the 11-amino acid linker region (169-179): a 70% reduction in luciferase reporter signal and a similar reduction in the level of viral RNA synthesis are observed	Dengue virus type 2

Organism

Organism	UniProt	Comment	Textmining
Dengue virus type 2	-	-	-
Dengue virus type 4	Q2YHF0	-	-

Synonyms

Synonyms	Comment	Organism
NS2B18NS3	NS3 protein covalently attached to 18 residues of the N22B cofactor region	Dengue virus type 2
NS2B18NS3	NS3 protein covalently attached to 18 residues of the N22B cofactor region	Dengue virus type 4

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Release 2023.1 (January 2023)