Domains mediating intramolecular folding and oligomerization of MxA GTPase.

@article{Schumacher1998DomainsMI,
  title={Domains mediating intramolecular folding and oligomerization of MxA GTPase.},
  author={Beat Schumacher and Peter Staeheli},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 43},
  pages={28365-70}
}
MxA is an interferon-induced GTPase of human cells that inhibits the multiplication of several RNA viruses by a still poorly understood mechanism. Previous biochemical studies indicated that the C terminus of MxA folds back to form a functional GTP-binding pocket, and that an internal fragment contains a domain required for oligomerization. Using the yeast two-hybrid system, we have now mapped these domains. MxA sequences located downstream of amino acid 564 were found to strongly interact with… CONTINUE READING
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