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 |
|---|---|
| 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