The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes

Cited 426 time in webofscience Cited 437 time in scopus
  • Hit : 502
  • Download : 0
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.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2003-12
Language
English
Article Type
Article
Keywords

INTERFERENCE; PROTEINS; PROGRAM; SIRNAS; REQUIREMENTS; MAINTENANCE; RECOGNITION; DROSOPHILA; MOLSCRIPT; SEQUENCES

Citation

NATURE STRUCTURAL BIOLOGY, v.10, no.12, pp.1026 - 1032

ISSN
1072-8368
DOI
10.1038/nsb1016
URI
http://hdl.handle.net/10203/83011
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 426 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0