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 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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