Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.

@article{Haller2010DynaminlikeMG,
  title={Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.},
  author={Otto Haller and Song Gao and Alexander von der Malsburg and Oliver Daumke and Georg Kochs},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 37},
  pages={28419-24}
}
The interferon-inducible MxA GTPase is a key mediator of cell-autonomous innate immunity against a broad range of viruses such as influenza and bunyaviruses. MxA shares a similar domain structure with the dynamin superfamily of mechanochemical enzymes, including an N-terminal GTPase domain, a central middle domain, and a C-terminal GTPase effector domain. Recently, crystal structures of a GTPase domain dimer of dynamin 1 and of the oligomerized stalk of MxA (built by the middle and GTPase… CONTINUE READING