RRM-RNA recognition: NMR or crystallography ... and new findings

被引:159
作者
Daubner, Gerrit M. [1 ]
Clery, Antoine [1 ]
Allain, Frederic H-T [1 ]
机构
[1] ETH, Inst Mol Biol & Biophys, Zurich, Switzerland
关键词
3' SPLICE-SITE; MOTOR-NEURON SMN; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; CONFORMATIONAL ENSEMBLES; HYDRATION DYNAMICS; TRACT RECOGNITION; EXON-7; INCLUSION; MOLECULAR-BASIS; PROTEIN;
D O I
10.1016/j.sbi.2012.11.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To characterize protein-RNA recognition at the molecular level, structural biology has turned out to be an indispensable approach. Detailed and direct insights into the mechanism of RNA binding and specificity have emerged from protein-RNA structures, especially from the most abundant RNA recognition motif (RRM). Although this protein domain has a very conserved alpha-beta fold, it can recognize a large number of different RNA sequences and shapes and can be involved in a multitude of biological processes. Here, we report on recent single and multiple RRM-RNA structures and point out those features that provide novel insights into the mechanism of RNA recognition by RRMs. We further outline inherent problems to both NMR spectroscopy and X-ray crystallography methods and review recent strategies that emphasize the need to use both methodologies for more rapid and accurate structure determinations.
引用
收藏
页码:100 / 108
页数:9
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