Crystal structure of unlinked NS2B-NS3 protease from Zika virus

Crystal structure of unlinked NS2B-NS3 protease from Zika virus

Zika virus (ZIKV) has rapidly emerged as a global public health concern. Viral NS2B-NS3 protease processes viral polyprotein and is essential for the virus replication, making it an attractive antiviral drug target. We report crystal structures at 1.58-angstrom resolution of the unlinked NS2B-NS3 pr...

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Bibliographic Details
Main Authors: Zhang, Zhenzhen, Li, Yan, Loh, Ying Ru, Phoo, Wint Wint, Hung, Alvin W., Kang, CongBao, Luo, Dahai
Other Authors: Lee Kong Chian School of Medicine (LKCMedicine)
Format: Article
Language:English
Published: 2017
Subjects:
Crystal Structure
Zika Virus
Online Access:https://hdl.handle.net/10356/84352
http://hdl.handle.net/10220/43576
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Institution: Nanyang Technological University
Language: English
Description
Summary:Zika virus (ZIKV) has rapidly emerged as a global public health concern. Viral NS2B-NS3 protease processes viral polyprotein and is essential for the virus replication, making it an attractive antiviral drug target. We report crystal structures at 1.58-angstrom resolution of the unlinked NS2B-NS3 protease from ZIKV as free enzyme and bound to a peptide reversely oriented at the active site. The unlinked NS2B-NS3 protease adopts a closed conformation in which NS2B engages NS3 to form an empty substrate-binding site. A second protease in the same crystal binds to the residues K14K15G16E17 from the neighboring NS3 in reverse orientation, resisting proteolysis. These features of ZIKV NS2B-NS3 protease may accelerate the discovery of structure-based antiviral drugs against ZIKV and related pathogenic flaviviruses.

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