Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979896 | Current Opinion in Structural Biology | 2008 | 9 Pages |
Abstract
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 α-helices on a four-stranded β-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 (β-strands, loops, α-helices). The extreme structural versatility of the RRM interactions explains why RRM-containing proteins have so diverse biological functions.
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Authors
Antoine Cléry, Markus Blatter, Frédéric H-T Allain,