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Structural Basis for Double-Stranded RNA Processing by Dicer
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.
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Cites
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Melet, L., Canan, J., Villalobos, P., Vidal-Veuthey, B., González-Toro, F., Orellana, I., Rivas-Pardo, J. A., Cárdenas, J. P., Moraga, C., Castro-Fernández, V., et al. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.11.009 · Cited by 1
Metadata
- Authors
- MacRae, I. J., Zhou, K., Li, F., Repic, A., Brooks, A. N., Cande, W. Z., Adams, P. D., & Doudna, J. A.
- Venue
- Science
- Published
- 2006-01-13
- Volume
- 311
- Issue
- 5758
- Pages
- 195-198
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2024316824
- Cited by
- 962
- References
- 2
- FWCI
- 21.12
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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