title: Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.
abstract: 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.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Lingel
authors.forename: Bernd
authors.initials: B
authors.lastname: Simon
authors.forename: Elisa
authors.initials: E
authors.lastname: Izaurralde
authors.forename: Michael
authors.initials: M
authors.lastname: Sattler
mesh_terms: 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
chemical_list: C433807:AGO2 protein, Drosophila; D060565:Argonaute Proteins; D029721:Drosophila Proteins; D009696:Nucleic Acids; D034741:RNA, Small Interfering; D034743:RNA-Induced Silencing Complex; D012996:Solutions