Key result
First solution structures of mouse RNA helicase A dsRBDs reveal binding and molecular reassembly insights.
First dsRBD structures of RNA helicase A; extends molecular insights into RNA binding, leaving cardiovascular relevance open.
RNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex. We present the first solution structures of the double-stranded RNA-binding domains (dsRBDs), dsRBD1 and dsRBD2, from mouse RHA. We discuss the binding mode of the dsRBDs of RHA, in comparison with the known dsRBD structures in their complexes. Our structural data provide important information for the elucidation of the molecular reassembly mediated by RHA.
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Nagata et al. (2012) studied this question. Structural analysis of dsRBD1 and dsRBD2 from mouse RHA was evaluated on Solution structures of dsRBD1 and dsRBD2. The first solution structures of the double-stranded RNA-binding domains (dsRBD1 and dsRBD2) from mouse RNA helicase A were determined, providing insights into its binding mode and molecular reassembly.
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