Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen.
NMR spectroscopy has been used to determine the secondary structure of one of the double-stranded RNA binding domains from the Drosophila protein staufen. The domain has an alpha beta beta beta alpha arrangement of secondary structure, with the beta strands forming an antiparallel beta sheet. The secondary structure differs from that found in the RNP RNA binding domain.
Bycroft
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M
Cambridge Centre for Protein Engineering, Department of Chemistry, University of Cambridge, UK.
Proctor
M
M
Freund
S M
SM
St Johnston
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D
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004330:Drosophila / Q000737:chemistry; D029721:Drosophila Proteins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012330:RNA, Double-Stranded / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism
D029721:Drosophila Proteins; D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; C069927:stau protein, Drosophila