Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Murray Valley encephalitis virus (MVEV), a mosquito-borne flavivirus endemic to Australia, is closely related to Japanese encephalitis virus and West Nile virus. Nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains, whose activity is central to flavivirus replication and is therefore a possible target for anti-flaviviral compounds. Cloning, purification, and crystal structure determination to 1.9 Angstrom resolution of the NS3 helicase of MVEV and characterization of its enzymatic activity is reported. Comparison with the structures of helicases from related viruses supports a possible mechanism of ATP hydrolysis-driven strand separation.
Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution.,Mancini EJ, Assenberg R, Verma A, Walter TS, Tuma R, Grimes JM, Owens RJ, Stuart DI Protein Sci. 2007 Oct;16(10):2294-300. PMID:17893366[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mancini EJ, Assenberg R, Verma A, Walter TS, Tuma R, Grimes JM, Owens RJ, Stuart DI. Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Angstrom resolution. Protein Sci. 2007 Oct;16(10):2294-300. PMID:17893366 doi:16/10/2294
