The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.

@article{Kostyuchenko2011TheSO,
  title={The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions.},
  author={Victor A. Kostyuchenko and Joanita Jakana and Xiangan Liu and Andrew D. Haddow and Myint Oo Aung and Scott C Weaver and Wah Chiu and Shee-Mei Lok},
  journal={Journal of virology},
  year={2011},
  volume={85 18},
  pages={
          9327-33
        }
}
Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-Å-resolution cryo-electron microscopy three-dimensional structure of BFV exhibits a typical alphavirus organization, with RNA-containing nucleocapsid surrounded by a bilipid membrane anchored with the surface proteins E1 and E2. The map allows details of the transmembrane regions of E1 and E2 to be seen. The C-terminal end of the E2 transmembrane helix binds to the capsid protein. Following the E2 transmembrane… CONTINUE READING

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