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

Andreas Lingel; Bernd Simon; Elisa Izaurralde; Michael Sattler

doi:10.1038/nsmb777

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

Andreas Lingel
, Bernd Simon
, Elisa Izaurralde
, Michael Sattler

European Molecular Biology Laboratory Heidelberg

Research output: Contribution to journal › Article › peer-review

272 Scopus citations

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 nucleolides 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.

Original language	English
Pages (from-to)	576-577
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	11
Issue number	6
DOIs	https://doi.org/10.1038/nsmb777
State	Published - Jun 2004
Externally published	Yes

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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 nucleolides 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.",

author = "Andreas Lingel and Bernd Simon and Elisa Izaurralde and Michael Sattler",

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AU - Lingel, Andreas

AU - Simon, Bernd

AU - Izaurralde, Elisa

AU - Sattler, Michael

PY - 2004/6

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N2 - 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 nucleolides 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.

AB - 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 nucleolides 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.

UR - https://www.scopus.com/pages/publications/2542461104

U2 - 10.1038/nsmb777

DO - 10.1038/nsmb777

M3 - Article

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SN - 1545-9993

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SP - 576

EP - 577

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 6

ER -

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

Abstract

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