tailieunhanh - Báo cáo khoa học: The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression

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 import-ant for binding a multitude of RNA sequences and proteins. | iFEBS Journal MINIREVIEW The RNA recognition motif a plastic RNA-binding platform to regulate post-transcriptional gene expression Christophe Maris Cyril Dominguez and Frederic . Allain Institute for Molecular Biology and Biophysics Swiss Federallnstitute of Technology Zurich ETH-Honggerberg Zurich Switzerland Keywords RNA recognition motif protein-RNA complex structure-function relationship RNA-binding specificity Correspondence F. . Allain Institute for Molecular Biology and Biophysics Swiss Federal Institute of Technology Zurich ETH-Honggerberg CH-8093 Zurich Switzerland Fax 41 1 6331294 Tel 41 1 6333940 E-mail allain@ Website http groups allain_group These authors contributed equally to the work 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 b-sheet the two external b-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. Received 16 December 2004 accepted 7 March 2005 doi History - what defines an RRM The RNA recognition motif RRM also known as the RNA-binding domain RBD or

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