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Title: The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression.
Authors: Maris, C
Dominguez, C
Allain, FH
First Published: May-2005
Citation: FEBS J, 2005, 272 (9), pp. 2118-2131
Abstract: 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.
DOI Link: 10.1111/j.1742-4658.2005.04653.x
ISSN: 1742-464X
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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