7v6c | pdb_00007v6c

Structure of the Dicer-2-R2D2 heterodimer bound to small RNA duplex

spinqualitylabelsall models 7v6c, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7v6c is a 6 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A1ZAW0_DROME] Publication Abstract from PubMed In flies, Argonaute2 (Ago2) and small interfering RNA (siRNA) form an RNA-induced silencing complex to repress viral transcripts(1). The RNase III enzyme Dicer-2 associates with its partner protein R2D2 and cleaves long double-stranded RNAs to produce 21-nucleotide siRNA duplexes, which are then loaded into Ago2 in a defined orientation(2-5). Here we report cryo-electron microscopy structures of the Dicer-2-R2D2 and Dicer-2-R2D2-siRNA complexes. R2D2 interacts with the helicase domain and the central linker of Dicer-2 to inhibit the promiscuous processing of microRNA precursors by Dicer-2. Notably, our structure represents the strand-selection state in the siRNA-loading process, and reveals that R2D2 asymmetrically recognizes the end of the siRNA duplex with the higher base-pairing stability, and the other end is exposed to the solvent and is accessible by Ago2. Our findings explain how R2D2 senses the thermodynamic asymmetry of the siRNA and facilitates the siRNA loading into Ago2 in a defined orientation, thereby determining which strand of the siRNA duplex is used by Ago2 as the guide strand for target silencing. Structure of the Dicer-2-R2D2 heterodimer bound to a small RNA duplex.,Yamaguchi S, Naganuma M, Nishizawa T, Kusakizako T, Tomari Y, Nishimasu H, Nureki O Nature. 2022 Jul;607(7918):393-398. doi: 10.1038/s41586-022-04790-2. Epub 2022, Jun 29. PMID:35768503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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