1R6Z: The Crystal Structure Of The Argonaute2 Paz Domain (as A Mbp Fusion)

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.
PDB ID: 1R6ZDownload
MMDB ID: 26170
PDB Deposition Date: 2003/10/17
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Similar Structures:
Biological Unit for 1R6Z: trimeric; determined by author and by software (PQS)
Molecular Components in 1R6Z
Label Count Molecule
Proteins (3 molecules)
Chimera of Maltose-binding Periplasmic Protein and Argonaute 2(Gene symbol: AGO2)
Molecule annotation
Chemicals (12 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB