RNA recognition motifs:: boring?: Not quite

被引:506
作者
Clery, Antoine [1 ]
Blatter, Markus [1 ]
Allain, Frederic H-T [1 ]
机构
[1] ETH, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland
关键词
D O I
10.1016/j.sbi.2008.04.002
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
The RNA recognition motif (RRM) is one of the most abundant protein domains in eukaryotes. While the structure of this domain is well characterized by the packing of two a-helices on a four-stranded P-sheet, the mode of protein and RNA recognition by RRMs is not clear owing to the high variability of these interactions. Here we report recent structural data on RRM-RNA and RRM-protein interactions showing the ability of this domain to modulate its binding affinity and specificity using each of its constitutive elements (P-strands, loops, a-helices). The extreme structural versatility of the RRM interactions explains why RRM-containing proteins have so diverse biological functions.
引用
收藏
页码:290 / 298
页数:9
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