Journal
SCIENCE
Volume 354, Issue 6319, Pages 1597-1600Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aai9309
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- Lee Kong Chian School of Medicine, Nanyang Technological University
- National Medical Research Council [CBRG15May045]
- A*STAR Joint Council Office [1431AFG102/1331A028]
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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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