Single-stranded-RNA binding proteins

Curr Opin Struct Biol. 2000 Feb;10(1):87-94. doi: 10.1016/s0959-440x(99)00054-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins*
  • Drosophila Proteins*
  • Drosophila melanogaster / metabolism
  • Escherichia coli / metabolism
  • Geobacillus stearothermophilus / metabolism
  • Humans
  • Models, Molecular
  • Nucleic Acid Conformation
  • Poly(A)-Binding Proteins
  • Protein Conformation
  • RNA / chemistry
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism*
  • Rho Factor / chemistry
  • Rho Factor / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism


  • Bacterial Proteins
  • Drosophila Proteins
  • MtrB protein, Bacteria
  • Poly(A)-Binding Proteins
  • RNA-Binding Proteins
  • Rho Factor
  • Sxl protein, Drosophila
  • Transcription Factors
  • RNA