Single-stranded-RNA binding proteins.
Our knowledge of protein interactions with RNA molecules has been, so far, largely restricted to cases in which the RNA itself is folded into a secondary and/or tertiary structure stabilised by intramolecular base pairing and stacking. Until recently, only limited structural information has been available about protein interactions with single-stranded RNA. A breakthrough in our understanding of these interactions came in 1999, with the determination of four crystal structures of protein complexes with extended single-stranded RNA molecules. These structures revealed wonderfully satisfying patterns of the ability of proteins to accommodate RNA bases, with the sugar-phosphate backbone often adopting conformations that are different from the classical double helix.
Antson
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York Structural Biology Laboratory, Department of Chemistry, University of York, York, YO10 5DD, UK. fred@yorvic.york.ac.uk
D000818:Animals; D001426:Bacterial Proteins; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D001411:Geobacillus stearothermophilus / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D039102:Poly(A)-Binding Proteins; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012234:Rho Factor / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D029721:Drosophila Proteins; C079092:MtrB protein, Bacteria; D039102:Poly(A)-Binding Proteins; D016601:RNA-Binding Proteins; D012234:Rho Factor; C067777:Sxl protein, Drosophila; D014157:Transcription Factors; D012313:RNA