Solution structures of the double‐stranded RNA‐binding domains from rna helicase A
Copyright policy )Solution structures of the double‐stranded RNA‐binding domains from rna helicase A
AbstractRNA 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. Proteins 2012;. © 2012 Wiley Periodicals, Inc.
- Goethe University Frankfurt Germany
- Yokohama City University Japan
- Kyoto University Japan
- Osaka University Japan
- Frankfurt Institute for Advanced Studies Germany
Models, Molecular, Binding Sites, Molecular Sequence Data, Solutions, Mice, Structure-Activity Relationship, Animals, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, RNA Helicases, RNA, Double-Stranded
Models, Molecular, Binding Sites, Molecular Sequence Data, Solutions, Mice, Structure-Activity Relationship, Animals, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, RNA Helicases, RNA, Double-Stranded
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