2wa2
From Proteopedia
Structure of the methyltransferase domain from Modoc Virus, a Flavivirus with No Known Vector (NKV)
Structural highlights
FunctionQ8QL64_9FLAV Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.[ARBA:ARBA00024317] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Modoc virus (MODV) is a flavivirus with no known vector (NKV). Evolutionary studies have shown that the viruses in the MODV group have evolved in association with mammals (bats, rodents) without transmission by an arthropod vector. MODV methyltransferase is the first enzyme from this evolutionary branch to be structurally characterized. The high-resolution structure of the methyltransferase domain of the MODV NS5 protein (MTase(MODV)) was determined. The protein structure was solved in the apo form and in complex with its cofactor S-adenosyl-L-methionine (SAM). Although it belongs to a separate evolutionary branch, MTase(MODV) shares structural characteristics with flaviviral MTases from the other branches. Its capping machinery is a relatively new target in flaviviral drug development and the observed structural conservation between the three flaviviral branches indicates that it may be possible to identify a drug that targets a range of flaviviruses. The structural conservation also supports the choice of MODV as a possible model for flavivirus studies. Structure of the methyltransferase domain from the Modoc virus, a flavivirus with no known vector.,Jansson AM, Jakobsson E, Johansson P, Lantez V, Coutard B, de Lamballerie X, Unge T, Jones TA Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):796-803. Epub 2009, Jul 10. PMID:19622863[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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