Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/83027
Title: | Structure of the NS2B-NS3 protease from Zika virus after self-cleavage | Authors: | Phoo, Wint Wint Li, Yan Zhang, Zhenzhen Lee, Michelle Yueqi Loh, Ying Ru Tan, Yaw Bia Ng, Elizabeth Yihui Lescar, Julien Kang, CongBao Luo, Dahai |
Keywords: | Zika virus NS2B-NS3 |
Issue Date: | 2016 | Source: | Phoo, W. W., Li, Y., Zhang, Z., Lee, M. Y., Loh, Y. R., Tan, Y. B., et al. (2016). Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. Nature Communications, 7, 13410-. | Series/Report no.: | Nature Communications | Abstract: | The recent outbreak of Zika virus (ZIKV) infections in the Americas represents a serious threat to the global public health. The viral protease that processes viral polyproteins during infection appears as an attractive drug target. Here we report a crystal structure at 1.84 Å resolution of ZIKV non-structural protein NS2B-NS3 protease with the last four amino acids of the NS2B cofactor bound at the NS3 active site. This structure represents a post-proteolysis state of the enzyme during viral polyprotein processing and provides insights into peptide substrate recognition by the protease. Nuclear magnetic resonance (NMR) studies and protease activity assays unravel the protein dynamics upon binding the protease inhibitor BPTI in solution and confirm this finding. The structural and functional insights of the ZIKV protease presented here should advance our current understanding of flavivirus replication and accelerate structure-based antiviral drug discovery against ZIKV. | URI: | https://hdl.handle.net/10356/83027 http://hdl.handle.net/10220/42379 |
ISSN: | 2041-1723 | DOI: | 10.1038/ncomms13410 | Schools: | School of Biological Sciences Lee Kong Chian School of Medicine (LKCMedicine) |
Research Centres: | NTU Institute of Structural Biology | Rights: | © 2016 The Author(s). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | Fulltext Permission: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | LKCMedicine Journal Articles SBS Journal Articles |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
ncomms13410.pdf | 1.27 MB | Adobe PDF | View/Open |
SCOPUSTM
Citations
5
159
Updated on Mar 21, 2024
Web of ScienceTM
Citations
5
151
Updated on Oct 27, 2023
Page view(s) 10
886
Updated on Mar 27, 2024
Download(s) 20
194
Updated on Mar 27, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.