Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 6, Pages 559-560Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1099
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Funding
- NCRR NIH HHS [P41 RR002250, P41 RR007707] Funding Source: Medline
- NIAID NIH HHS [AI07471, R01 AI036040, AI36040, R37 AI036040, P01 AI057788] Funding Source: Medline
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The nonstructural protein NS1 of influenza virus is an antagonist of host immune responses and is implicated in virulence. It has two domains, an N-terminal double-stranded RNA-binding domain (RBD) and an effector domain crucial for RBD function, for nuclear export and for sequestering messenger RNA-processing proteins. Here we present the crystallographic structure of the effector domain, which has a novel fold and suggests mechanisms for increased virulence in H5N1 strains.
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