Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid association.

@article{Hartlieb2007CrystalSO,
  title={Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid association.},
  author={Bettina Hartlieb and Tadeusz Muziol and Winfried Weissenhorn and Stephan Becker},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 2},
  pages={624-9}
}
Transcription of the highly pathogenic Ebola virus depends on VP30, a nucleocapsid-associated Ebola virus-specific transcription factor. The transcription activator VP30 was shown to play an essential role in Ebola virus replication, most likely by stabilizing nascent mRNA. Here we present the crystal structure of the C-terminal domain (CTD) of VP30 (VP30(CTD)) at 2.0-A resolution. VP30(CTD) folds independently into a dimeric helical assembly. The VP30(CTD) dimers assemble into hexamers that… CONTINUE READING
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