2kou

DICER LIKE protein

spinqualitylabelsall models 2kou Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kou is a 1 chain structure with sequence from Arabidopsis thaliana. 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 DCL4_ARATH Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the biogenesis of trans-acting small interfering RNAs (ta-siRNAs, derived from the TAS1, TAS2 or TAS3 endogenous transcripts) by cleaving small dsRNAs into 21-24 nucleotide ta-siRNAs. Functions with the dsRNA-binding protein DRB4 in ta-siRNAs processing. Acts in the RDR6/SGS3/DCL4/AGO7 ta-siRNA pathway involved in leaf developmental timing. Plays a role in transitive silencing of transgenes by processing secondary siRNAs. This pathway, which requires DCL2 and RDR6, amplifies silencing by using the target RNA as substrate to generate secondary siRNAs, providing an efficient mechanism for long-distance silencing. Required for the production of the 30-40 nucleotide bacterial-induced long siRNAs (lsiRNA). May participate with DCL3 in the production of 24 nucleotide repeat-associated siRNAs (ra-siRNAs) which derive from heterochromatin and DNA repeats such as transposons. Plays an important role in antiviral RNA silencing. Involved in the production of viral siRNAs derived from the cucumber mosaic virus (CMV), turnip crinkle virus (TCV) and tobacco rattle virus (TRV). Targeted by the viral silencing suppressor (VSR) protein 2b of the cucumber mosaic virus (CMV) that inactivates DCL4 function in RNA silencing. Does not seem to be involved in microRNAs (miRNAs) processing. 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 Dicer or Dicer-like (DCL) protein is a catalytic component involved in microRNA (miRNA) or small interference RNA (siRNA) processing pathway, whose fragment structures have been partially solved. However, the structure and function of the unique DUF283 domain within dicer is largely unknown. Here we report the first structure of the DUF283 domain from the Arabidopsis thaliana DCL4. The DUF283 domain adopts an alpha-beta-beta-beta-alpha topology and resembles the structural similarity to the double-stranded RNA-binding domain. Notably, the N-terminal alpha helix of DUF283 runs cross over the C-terminal alpha helix orthogonally, therefore, N- and C-termini of DUF283 are in close proximity. Biochemical analysis shows that the DUF283 domain of DCL4 displays weak dsRNA binding affinity and specifically binds to double-stranded RNA-binding domain 1 (dsRBD1) of Arabidopsis DRB4, whereas the DUF283 domain of DCL1 specifically binds to dsRBD2 of Arabidopsis HYL1. These data suggest a potential functional role of the Arabidopsis DUF283 domain in target selection in small RNA processing. Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a noncanonical double-stranded RNA-binding fold for protein-protein interaction.,Qin H, Chen F, Huan X, Machida S, Song J, Yuan YA RNA. 2010 Mar;16(3):474-81. Epub 2010 Jan 27. PMID:20106953 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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