ArticleInternational journal of molecular sciences2015
Novel Insights into Guide RNA 5'-Nucleoside/Tide Binding by Human Argonaute 2.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Comparative structural insights and functional analysis for the distinct unbound states of Human AGO proteins.Scientific reports · 2025Article
- A programmable pAgo nuclease with RNA target-cleavage specificity from the mesophilic bacteriumActa biochimica et biophysica Sinica · 2023Article
- RNA-protein complexes and force field polarizability.Frontiers in chemistry · 2023Article
- RNA-induced initiation of transcriptional silencing (RITS) complex structure and function.RNA biology · 2019Review
- Exploring PAZ/3'-overhang interaction to improve siRNA specificity. A combined experimental and modeling study.Chemical science · 2018Article
- Autonomous Generation and Loading of DNA Guides by Bacterial Argonaute.Molecular cell · 2017Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The human Argonaute 2 (hAgo2) protein is a key player of RNA interference (RNAi). Upon complex formation with small non-coding RNAs, the protein initially interacts with the 5'-end of a given guide RNA through multiple interactions within the MID domain. This interaction has been reported to show a strong bias for U and A over C and G at the 5'-position. Performing molecular dynamics simulations of binary hAgo2/OH-guide-RNA complexes, we show that hAgo2 is a highly flexible protein capable of binding to guide strands with all four possible 5'-bases. Especially, in the case of C and G this is associated with rather large individual conformational rearrangements affecting the MID, PAZ and even the N-terminal domains to different degrees. Moreover, a 5'-G induces domain motions in the protein, which trigger a previously unreported interaction between the 5'-base and the L2 linker domain. Combining our in silico analyses with biochemical studies of recombinant hAgo2, we find that, contrary to previous observations, hAgo2 is capable of functionally accommodating guide strands regardless of the 5'-base.
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