Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.
We describe the solution structures of the Argonaute2 PAZ domain bound to RNA and DNA oligonucleotides. The structures reveal a unique mode of single-stranded nucleic acid binding in which the two 3'-terminal nucleotides are buried in a hydrophobic cleft. We propose that the PAZ domain contributes to the specific recognition of siRNAs by providing a binding pocket for their characteristic two-nucleotide 3' overhangs.
Lingel
Andreas
A
European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
Simon
Bernd
B
Izaurralde
Elisa
E
Sattler
Michael
M
D060565:Argonaute Proteins; D001665:Binding Sites; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D009696:Nucleic Acids / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D034741:RNA, Small Interfering / Q000378:metabolism; D034743:RNA-Induced Silencing Complex / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions
C433807:AGO2 protein, Drosophila; D060565:Argonaute Proteins; D029721:Drosophila Proteins; D009696:Nucleic Acids; D034741:RNA, Small Interfering; D034743:RNA-Induced Silencing Complex; D012996:Solutions