Ontology highlight
ABSTRACT:
SUBMITTER: Amaro RE
PROVIDER: S-EPMC3144582 | biostudies-literature | 2011 Jul
REPOSITORIES: biostudies-literature
Amaro Rommie E RE Swift Robert V RV Votapka Lane L Li Wilfred W WW Walker Ross C RC Bush Robin M RM
Nature communications 20110712
The recently discovered 150-cavity in the active site of group-1 influenza A neuraminidase (NA) proteins provides a target for rational structure-based drug development to counter the increasing frequency of antiviral resistance in influenza. Surprisingly, the 2009 H1N1 pandemic virus (09N1) neuraminidase was crystalized without the 150-cavity characteristic of group-1 NAs. Here we demonstrate, through a total sum of 1.6 μs of biophysical simulations, that 09N1 NA exists in solution preferential ...[more]