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Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2

Author

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  • Filipp Frank

    (McGill University, Montréal, Québec H3G 0B1, Canada
    Goodman Cancer Center, McGill University, Montréal, Québec H3G 0B1, Canada
    Groupe de Recherche Axe sur la Structure des Proteines, Montréal, Québec H3G 0B1, Canada)

  • Nahum Sonenberg

    (McGill University, Montréal, Québec H3G 0B1, Canada
    Goodman Cancer Center, McGill University, Montréal, Québec H3G 0B1, Canada)

  • Bhushan Nagar

    (McGill University, Montréal, Québec H3G 0B1, Canada
    Groupe de Recherche Axe sur la Structure des Proteines, Montréal, Québec H3G 0B1, Canada)

Abstract

Messenger RNAs: an end in the MIDdle The association of small RNAs, such as microRNAs (miRNAs), with Argonaute (AGO) family proteins yields complexes that regulate gene expression. While bacterial and archaeal miRNAs show no sequence preference at their 5′ ends, eukaryotic miRNAs tend to have 5′ U or A. To determine the basis of this preference, Bhushan Nagar and colleagues have solved the structure of the human AGO2 MID domain complexed with ribonucleotide monophosphates. The structure reveals a specific interaction of UMP and AMP with a loop that also discriminates against CMP or GMP.

Suggested Citation

  • Filipp Frank & Nahum Sonenberg & Bhushan Nagar, 2010. "Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2," Nature, Nature, vol. 465(7299), pages 818-822, June.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7299:d:10.1038_nature09039
    DOI: 10.1038/nature09039
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    Cited by:

    1. Sucharita Sarkar & Samarjit Das & SudipRoy & Dilip Pahari & Arpita Ghosh Mitra, 2016. "Exosomal Consignment in Renal Allograft Injury," International Journal of Cell Science & Molecular Biology, Juniper Publishers Inc., vol. 1(1), pages 1-6, March.

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