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Nucleic acid 3′-end recognition by the Argonaute2 PAZ domain

Nature Structural & Molecular Biology volume 11, pages 576–577 (2004)Cite this article

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.

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Figure 1: Structure of the Ago2 PAZ domain bound to a pentamer DNA or RNA oligonucleotide.
Figure 2: Details of nucleic acid recognition.

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Acknowledgements

We thank G. Stier and S. Bäckström for the pETM60 vector, M. Nilges for discussions, H. Siomi for the Ago2 cDNA, the Center for Biomolecular Magnetic Resonance (BMRZ) in Frankfurt for NMR measurement time, and Biospring (Frankfurt) for RNA synthesis. This study was supported by the European Molecular Biology Organization, the German Research Foundation, the European Union and the Human Frontier Science Program Organization.

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  1. European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, D-69117, Germany

    Andreas Lingel, Bernd Simon, Elisa Izaurralde & Michael Sattler

Authors
  1. Andreas Lingel
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  2. Bernd Simon
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  3. Elisa Izaurralde
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  4. Michael Sattler
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Correspondence to Elisa Izaurralde or Michael Sattler.

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The authors declare no competing financial interests.

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Lingel, A., Simon, B., Izaurralde, E. et al. Nucleic acid 3′-end recognition by the Argonaute2 PAZ domain. Nat Struct Mol Biol 11, 576–577 (2004). https://doi.org/10.1038/nsmb777

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