Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design.

@article{Ng2008StructureOT,
  title={Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design.},
  author={Andy Ka-Leung Ng and Hongmin Zhang and Kemin Tan and Zongli Li and Jin-huan Liu and Paul K S Chan and S Li and Wood-yee Chan and Shannon Wing Ngor Au and Andrzej Joachimiak and Thomas Walz and Jia-Huai Wang and P Shaw},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2008},
  volume={22 10},
  pages={3638-47}
}
The threat of a pandemic outbreak of influenza virus A H5N1 has become a major concern worldwide. The nucleoprotein (NP) of the virus binds the RNA genome and acts as a key adaptor between the virus and the host cell. It, therefore, plays an important structural and functional role and represents an attractive drug target. Here, we report the 3.3-A crystal structure of H5N1 NP, which is composed of a head domain, a body domain, and a tail loop. Our structure resolves the important linker… CONTINUE READING
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