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Crystal Structure of Dicer from Giardia intestinalisCrystal Structure of Dicer from Giardia intestinalis
Structural highlights
Publication Abstract from PubMedThe 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. Structural basis for double-stranded RNA processing by Dicer.,Macrae IJ, Zhou K, Li F, Repic A, Brooks AN, Cande WZ, Adams PD, Doudna JA Science. 2006 Jan 13;311(5758):195-8. PMID:16410517[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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