ArticleJournal of computational chemistry2026
How Do DICER1 Syndrome Mutations Disrupt Catalysis? Unveiling Dicer Metal Binding Architecture and Mechanism of Action Using MD Simulations and QM/MM Calculations.
Article in Journal of computational chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The RNA interference (RNAi) pathway regulates gene expression and viral defense and has been harnessed in therapeutic solutions to inhibit otherwise undruggable proteins by preventing translation. Dicer initiates RNAi by generating cleaved RNA products that bind to a target mRNA to promote gene silencing. Mutations to the Dicer catalytic domain cause DICER1 syndrome, which increases the risk of cancers, including early childhood variants. However, the catalytic mechanism remains poorly defined due to the lack of structural data for Dicer bound to a substrate (or substrate mimic) in the presence of divalent ions known to be critical for nuclease activity. This study uses molecular dynamics (MD) simulations to uncover the first atomic level structure of the wild-type Dicer-RNA complex, including the binding pattern of two catalytically essential Mg
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