1t2s

Structural basis for 3' end recognition of nucleic acids by the Drosophila Argonaute 2 PAZ domainStructural basis for 3' end recognition of nucleic acids by the Drosophila Argonaute 2 PAZ domain

Structural highlights 1t2s is a 2 chain structure with sequence from Drosophila melanogaster. 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 We describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3'-terminal nucleotides are buried in a hydrophobic cleft. We propose that the PAZ domain contributes to the specific recognition of siRNAs by providing a binding pocket for their characteristic two-nucleotide 3' overhangs. Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.,Lingel A, Simon B, Izaurralde E, Sattler M Nat Struct Mol Biol. 2004 Jun;11(6):576-7. Epub 2004 May 23. PMID:15156196 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Argonaute 3D structures

spinqualitylabelsall models 1t2s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image