Structural Basis for Double-Stranded RNA Processing by Dicer
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- 13 January 2006
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 311 (5758) , 195-198
- https://doi.org/10.1126/science.1121638
Abstract
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. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.Keywords
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