Structural Basis for Double-Stranded RNA Processing by Dicer

@article{MacRae2006StructuralBF,
  title={Structural Basis for Double-Stranded RNA Processing by Dicer},
  author={Ian J. MacRae and Kaihong Zhou and Fei Li and Adrian Repic and Angela N. Brooks and William Zacheus Cande and Paul D. Adams and Jennifer A. Doudna},
  journal={Science},
  year={2006},
  volume={311},
  pages={195 - 198}
}
The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA… Expand
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