| Literature DB >> 16270100 |
Andreas Lingel1, Bernd Simon, Elisa Izaurralde, Michael Sattler.
Abstract
We report the structure of the flock house virus B2 protein, a potent suppressor of RNA interference (RNAi) in animals and plants. The B2 protein is a homodimer in solution and contains three alpha-helices per monomer. Chemical shift perturbation shows that an antiparallel arrangement of helices (alpha2/alpha2') forms an elongated binding interface with double-stranded RNA (dsRNA). This implies a novel mode of dsRNA recognition and provides insights into the mechanism of RNAi suppression by B2.Entities:
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Year: 2005 PMID: 16270100 PMCID: PMC1369214 DOI: 10.1038/sj.embor.7400583
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807