1VYN

STRUCTURE AND NUCLEIC ACID BINDING OF THE DROSOPHILA ARGONAUTE2 PAZ DOMAIN

Replaces:  1UPO

Summary for 1VYN

• Entry DOI: 10.2210/pdb1vyn/pdb
• Related: 1R6Z
• Descriptor: ARGONAUTE2 (1 entity in total)
• Functional Keywords: nucleic acid binding, rna interference
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Total number of polymer chains: 1
• Total formula weight: 16066.42

Authors

Lingel, A.,Simon, B.,Izaurralde, E.,Sattler, M. (deposition date: 2004-05-03, release date: 2004-05-11, Last modification date: 2024-05-15)

Primary citation

Lingel, A.,Simon, B.,Izaurralde, E.,Sattler, M.
Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain.
Nature, 426:465-469, 2003

PubMed Abstract: 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.

PubMed: 14615801
DOI: 10.1038/nature02123

Experimental method

SOLUTION NMR