Please use this identifier to cite or link to this item:
|Title:||The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression.|
|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.|
|Appears in Collections:||Published Articles, Dept. of Biochemistry|
Files in This Item:
There are no files associated with this item.
Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.