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lüll The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression Maris C; Dominguez C; Allain FHFEBS J 2005[May]; 272 (9): 2118-31The 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.|*Amino Acid Sequence[MESH]|*Gene Expression Regulation[MESH]|*Protein Biosynthesis[MESH]|*Protein Conformation[MESH]|*Protein Folding[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Protein Binding[MESH]|RNA/metabolism[MESH]|Sequence Alignment[MESH] |