@article{PAR00006540,
  title = {{S}tructure of the methyltransferase domain from the {M}odoc virus, a flavivirus with no known vector},
  author = {{J}ansson, {A}. {M}. and {J}akobsson, {E}. and {J}ohansson, {P}. and {L}antez, {V}. and {C}outard, {B}. and de {L}amballerie, {X}avier and {U}nge, {T}. and {J}ones, {T}. {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he {M}odoc virus ({MODV}) is a flavivirus with no known vector ({NKV}). {E}volutionary 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. {T}he high-resolution structure of the methyltransferase domain of the {MODV} {NS}5 protein ({MT}ase({MODV})) was determined. {T}he protein structure was solved in the apo form and in complex with its cofactor {S}-adenosyl-l-methionine ({SAM}). {A}lthough it belongs to a separate evolutionary branch, {MT}ase({MODV}) shares structural characteristics with flaviviral {MT}ases from the other branches. {I}ts 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. {T}he structural conservation also supports the choice of {MODV} as a possible model for flavivirus studies.},
  keywords = {},
  booktitle = {},
  journal = {{A}cta {C}rystallographica {S}ection {D}. {B}iological {C}rystallography},
  volume = {65},
  numero = {{P}art 8},
  pages = {796--803},
  ISSN = {0907-4449},
  year = {2009},
  DOI = {10.1107/s0907444909017260},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00006540},
}