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 α-helices per monomer. Chemical shift perturbation shows that an antiparallel arrangement of helices (α2/α2′) 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.
Original language | English |
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Pages (from-to) | 1149-1155 |
Number of pages | 7 |
Journal | EMBO Reports |
Volume | 6 |
Issue number | 12 |
DOIs | |
State | Published - Dec 2005 |
Externally published | Yes |
Keywords
- RNAi
- Viral suppressor
- dsRNA recognition