title: Solution structures of the double-stranded RNA-binding domains from RNA helicase A.
abstract: 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.
authors.affiliation: Institute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Nagata
authors.forename: Kengo
authors.initials: K
authors.lastname: Tsuda
authors.forename: Naohiro
authors.initials: N
authors.lastname: Kobayashi
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Takanori
authors.initials: T
authors.lastname: Kigawa
authors.forename: Peter
authors.initials: P
authors.lastname: Güntert
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Muto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D020365:RNA Helicases / Q000737:chemistry* / Q000378:metabolism*; D012330:RNA, Double-Stranded / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D012996:Solutions; D013329:Structure-Activity Relationship
chemical_list: D012330:RNA, Double-Stranded; D012996:Solutions; D020365:RNA Helicases