title: Structure of the RNA-binding domain of Nodamura virus protein B2, a suppressor of RNA interference.
abstract: Protein B2 from Nodamura virus (NMV B2), a member of the Nodavirus family, acts as a suppressor of RNA interference (RNAi). The N-terminal domain of NMV B2, consisting of residues 1-79, recognizes double-stranded RNA (dsRNA). The 2.5 A crystal structure of the RNA-binding domain of NMV B2 shows a dimeric, helical bundle structure. The structure shows a conserved set of RNA-binding residues compared with flock house virus B2, despite limited sequence identity. The crystal packing places the RNA-binding residues along one face of symmetry-related molecules, suggesting a potential platform for recognition of dsRNA.
authors.affiliation: Institute of Biophysical Chemistry, Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt, Germany.
authors.forename: Stephanie
authors.initials: S
authors.lastname: Körber
authors.forename: P
authors.initials: P
authors.lastname: Shaik Syed Ali
authors.forename: Julian C-H
authors.initials: JC
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D030381:Nodaviridae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D012330:RNA, Double-Stranded / Q000737:chemistry; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D012330:RNA, Double-Stranded; D014764:Viral Proteins