Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding

@inproceedings{Wu2013InducedOO,
  title={Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding},
  author={Yan Wu and Guangrong Qin and Feng Gao and Yue Liu and Christopher John Vavricka and Jianxun Qi and Hualiang Jiang and Kunqian Yu and George F. Gao},
  booktitle={Scientific reports},
  year={2013}
}
The recently discovered 150-cavity (formed by loop residues 147-152, N2 numbering) adjacent to the enzymatic active site of group 1 influenza A neuraminidase (NA) has introduced a novel target for the design of next-generation NA inhibitors. However, only group 1 NAs, with the exception of the 2009 pandemic H1N1 NA, possess a 150-cavity, and no 150-cavity has been observed in group 2 NAs. The role of the 150-cavity played in enzymatic activity and inhibitor binding is not well understood. Here… CONTINUE READING