[HTML][HTML] Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase
H Dong, L Liu, G Zou, Y Zhao, Z Li, SP Lim… - Journal of biological …, 2010 - ASBMB
The flavivirus methyltransferase (MTase) sequentially methylates the N7 and 2′-O
positions of the viral RNA cap (GpppA-RNA→ m 7 GpppA-RNA→ m 7 GpppAm-RNA), using
S-adenosyl-l-methionine (AdoMet) as a methyl donor. We report here that sinefungin (SIN),
an AdoMet analog, inhibits several flaviviruses through suppression of viral MTase. The
crystal structure of West Nile virus MTase in complex with SIN inhibitor at 2.0-Å resolution
revealed a flavivirus-conserved hydrophobic pocket located next to the AdoMet-binding site …
positions of the viral RNA cap (GpppA-RNA→ m 7 GpppA-RNA→ m 7 GpppAm-RNA), using
S-adenosyl-l-methionine (AdoMet) as a methyl donor. We report here that sinefungin (SIN),
an AdoMet analog, inhibits several flaviviruses through suppression of viral MTase. The
crystal structure of West Nile virus MTase in complex with SIN inhibitor at 2.0-Å resolution
revealed a flavivirus-conserved hydrophobic pocket located next to the AdoMet-binding site …