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- W1567447281 abstract "• Splicing factors contain different RNA-binding domains: RNA-recognition motif (RRM), KH domain, and Zn-finger. • The affinity of the RNA-binding domains for RNA can vary between 1 nM and 20 µM. • RNA-binding domains can also serve as protein–protein interaction domains. • The RRM is the most common RNA-binding motif. Although most of the RRMs interact with RNA by using the β-sheet surface, they are able to modulate their binding specificity and affinity using other constitutive elements (N- and C-terminal extremities, loops, and α-helices). • Detailed structural studies of splicing factors in complex with their RNA targets showed how they can discriminate seemingly similar sequences; for example, the recognition of polypyrimidine tracts by PTB, U2AF and Sex-lethal, and also suggested possible modes of splicing factor action." @default.
- W1567447281 created "2016-06-24" @default.
- W1567447281 creator A5015808138 @default.
- W1567447281 creator A5037966423 @default.
- W1567447281 date "2012-01-11" @default.
- W1567447281 modified "2023-09-26" @default.
- W1567447281 title "A Structural Biology Perspective of Proteins Involved in Splicing Regulation" @default.
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- W1567447281 doi "https://doi.org/10.1002/9783527636778.ch4" @default.
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