1r6z
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The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion)
OverviewOverview
RISC, the RNA-induced silencing complex, uses short interfering RNAs, (siRNAs) or micro RNAs (miRNAs) to select its targets in a, sequence-dependent manner. Key RISC components are Argonaute proteins, which contain two characteristic domains, PAZ and PIWI. PAZ is highly, conserved and is found only in Argonaute proteins and Dicer. We have, solved the crystal structure of the PAZ domain of Drosophila Argonaute2., The PAZ domain contains a variant of the OB fold, a module that often, binds single-stranded nucleic acids. PAZ domains show low-affinity nucleic, acid binding, probably interacting with the 3' ends of single-stranded, regions of RNA. PAZ can bind the characteristic two-base 3' overhangs of, siRNAs, indicating that although PAZ may not be a primary nucleic acid, binding site in Dicer or RISC, it may contribute to the specific and, productive incorporation of siRNAs and miRNAs into the RNAi pathway.
About this StructureAbout this Structure
1R6Z is a Single protein structure of sequence from Escherichia coli, drosophila melanogaster with MAL and NI as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes., Song JJ, Liu J, Tolia NH, Schneiderman J, Smith SK, Martienssen RA, Hannon GJ, Joshua-Tor L, Nat Struct Biol. 2003 Dec;10(12):1026-32. Epub 2003 Nov 16. PMID:14625589
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