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Structural characterization of the linked NS 2B‐ NS 3 protease of Zika virus
Author(s) -
Li Yan,
Phoo Wint Wint,
Loh Ying Ru,
Zhang Zhenzhen,
Ng Elizabeth Yihui,
Wang Weiling,
Keller Thomas H.,
Luo Dahai,
Kang CongBao
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12741
Subject(s) - protease , linker , chemistry , biochemistry , stereochemistry , enzyme , computer science , operating system
The Zika virus ( ZIKV ) NS 2B‐ NS 3 protease is an important drug target. The conventional flaviviral protease constructs used for structural studies contain the NS 2B cofactor region linked to the NS 3 protease domain via a glycine‐rich flexible linker. Here, we examined the structural dynamics of this conventional Zika protease (gZiPro) using NMR spectroscopy. Although the glycine‐rich linker in gZiP ro does not alter the overall folding of the protease in solution, gZiP ro 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. Our study provides a direct comparison of ZIKV protease constructs with and without an artificial linker.