Literature summary for 3.4.21.91 extracted from

Li, Y.; Phoo, W.W.; Loh, Y.R.; Zhang, Z.; Ng, E.Y.; Wang, W.; Keller, T.H.; Luo, D.; Kang, C.
Structural characterization of the linked NS2B-NS3 protease of Zika virus (2017), FEBS Lett., 591, 2338-2347 .

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Protein Variants

Protein Variants	Comment	Organism
additional information	construction of the NS2B cofactor region linked to the NS3 protease domain via a glycine-rich flexible linker (Gly4-Ser-Gly4 linker), structural dynamics of this conventional Zika protease (gZiPro) using NMR spectroscopy, overview. Although the glycine-rich linker in gZiPro does not alter the overall folding of the protease in solution, gZiPro is not homogenous in ion exchange chromatography. Compared to the unlinked protease construct, the artificial linker affects the chemical environment of many residues including H51 in the catalytic triad. Direct comparison of ZIKV protease constructs with and without an artificial linker, namely gZiPro (with the Gly4-Ser-Gly4 linker), bZiPro (unlinked NS2B NS3protease), and eZiPro (NS2B-NS3 junction sequence KTGKR as the linker). Solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation. Effect of the linker on the chemical environment of residues, dynamics of the linked protease, overview	Zika virus

Inhibitors

Inhibitors	Comment	Organism	Structure
AcKR-H	-	Zika virus

Organism

Organism	UniProt	Comment	Textmining
Zika virus	-	ZIKV	-

Synonyms

Synonyms	Comment	Organism
NS2B-NS3 protease	-	Zika virus

Cofactor

Cofactor	Comment	Organism	Structure
NS2B cofactor	essential	Zika virus

General Information

General Information	Comment	Organism
additional information	solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation	Zika virus

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Release 2023.1 (January 2023)