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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Argonaute Proteins
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Binding Sites
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Drosophila Proteins / chemistry*
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Drosophila Proteins / metabolism
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Nuclear Magnetic Resonance, Biomolecular
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Nucleic Acids / metabolism*
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Protein Binding
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Protein Conformation
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RNA, Small Interfering / metabolism
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RNA-Induced Silencing Complex / chemistry*
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RNA-Induced Silencing Complex / metabolism
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Solutions
Substances
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AGO2 protein, Drosophila
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Argonaute Proteins
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Drosophila Proteins
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Nucleic Acids
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RNA, Small Interfering
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RNA-Induced Silencing Complex
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Solutions