Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of unlinked NS2B-NS3 protease from Zika virus.,Zhang Z, Li Y, Loh YR, Phoo WW, Hung AW, Kang C, Luo D Science. 2016 Dec 23;354(6319):1597-1600. doi: 10.1126/science.aai9309. Epub 2016, Dec 8. PMID:27940580[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Z, Li Y, Loh YR, Phoo WW, Hung AW, Kang C, Luo D. Crystal structure of unlinked NS2B-NS3 protease from Zika virus. Science. 2016 Dec 23;354(6319):1597-1600. doi: 10.1126/science.aai9309. Epub 2016, Dec 8. PMID:27940580 doi:http://dx.doi.org/10.1126/science.aai9309
