1vyn

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STRUCTURE AND NUCLEIC ACID BINDING OF THE DROSOPHILA ARGONAUTE2 PAZ DOMAIN

Overview

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.

About this Structure

1VYN is a Single protein structure of sequence from Drosophila melanogaster. This structure superseeds the now removed PDB entry 1UPO. Full crystallographic information is available from OCA.

Reference

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

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