The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression

FEBS J. 2005 May;272(9):2118-31. doi: 10.1111/j.1742-4658.2005.04653.x.


The RNA recognition motif (RRM), also known as RNA-binding domain (RBD) or ribonucleoprotein domain (RNP) is one of the most abundant protein domains in eukaryotes. Based on the comparison of more than 40 structures including 15 complexes (RRM-RNA or RRM-protein), we reviewed the structure-function relationships of this domain. We identified and classified the different structural elements of the RRM that are important for binding a multitude of RNA sequences and proteins. Common structural aspects were extracted that allowed us to define a structural leitmotif of the RRM-nucleic acid interface with its variations. Outside of the two conserved RNP motifs that lie in the center of the RRM beta-sheet, the two external beta-strands, the loops, the C- and N-termini, or even a second RRM domain allow high RNA-binding affinity and specific recognition. Protein-RRM interactions that have been found in several structures reinforce the notion of an extreme structural versatility of this domain supporting the numerous biological functions of the RRM-containing proteins.

Publication types

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

MeSH terms

  • Amino Acid Sequence*
  • Gene Expression Regulation*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Biosynthesis*
  • Protein Conformation*
  • Protein Folding*
  • RNA / metabolism
  • Sequence Alignment


  • RNA