Structural highlights
Function
A0A109PRQ3_ZIKV Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504]
Publication Abstract from PubMed
The association of Zika virus (ZIKV) infections with microcephaly has resulted in an ongoing public-health emergency. Here we report the crystal structure of a C-terminal fragment of ZIKV nonstructural protein 1 (NS1), a major host-interaction molecule that functions in flaviviral replication, pathogenesis and immune evasion. Comparison with West Nile and dengue virus NS1 structures reveals conserved features but diverse electrostatic characteristics at host-interaction interfaces, thus possibly implying different modes of flavivirus pathogenesis.
Zika virus NS1 structure reveals diversity of electrostatic surfaces among flaviviruses.,Song H, Qi J, Haywood J, Shi Y, Gao GF Nat Struct Mol Biol. 2016 May;23(5):456-8. doi: 10.1038/nsmb.3213. Epub 2016 Apr , 18. PMID:27088990[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song H, Qi J, Haywood J, Shi Y, Gao GF. Zika virus NS1 structure reveals diversity of electrostatic surfaces among flaviviruses. Nat Struct Mol Biol. 2016 May;23(5):456-8. doi: 10.1038/nsmb.3213. Epub 2016 Apr , 18. PMID:27088990 doi:http://dx.doi.org/10.1038/nsmb.3213
