1vyn | pdb_00001vyn

STRUCTURE AND NUCLEIC ACID BINDING OF THE DROSOPHILA ARGONAUTE2 PAZ DOMAIN

spinqualitylabelsall models 1vyn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vyn is a 1 chain structure with sequence from Drosophila melanogaster. This structure supersedes the now removed PDB entry 1upo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AGO2_DROME Essential for RNA interference (RNAi); double-stranded RNA induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed RNA interference is a conserved mechanism that regulates gene expression in response to the presence of double-stranded (ds)RNAs. The RNase III-like enzyme Dicer first cleaves dsRNA into 21-23-nucleotide small interfering RNAs (siRNAs). In the effector step, the multimeric RNA-induced silencing complex (RISC) identifies messenger RNAs homologous to the siRNAs and promotes their degradation. The Argonaute 2 protein (Ago2) is a critical component of RISC. Both Argonaute and Dicer family proteins contain a common PAZ domain whose function is unknown. Here we present the three-dimensional nuclear magnetic resonance structure of the Drosophila melanogaster Ago2 PAZ domain. This domain adopts a nucleic-acid-binding fold that is stabilized by conserved hydrophobic residues. The nucleic-acid-binding patch is located in a cleft between the surface of a central beta-barrel and a conserved module comprising strands beta3, beta4 and helix alpha3. Because critical structural residues and the binding surface are conserved, we suggest that PAZ domains in all members of the Argonaute and Dicer families adopt a similar fold with nucleic-acid binding function, and that this plays an important part in gene silencing. Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain.,Lingel A, Simon B, Izaurralde E, Sattler M Nature. 2003 Nov 27;426(6965):465-9. Epub 2003 Nov 16. PMID:14615801 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Argonaute 3D structures

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