Abstract
Cryo-electron microscopy has greatly advanced our understanding of how the spliceosome cycles through different conformational states to conduct the chemical reactions that remove introns from pre-mRNA transcripts. The Cryo-EM structures were built upon decades of crystallographic studies of various spliceosomal RNA-protein complexes. In this review we give an overview of the crystal structures solved in the Nagai group, utilizing many of the strategies to design crystal packing as described in the accompanying paper.
Highlights
The spliceosome is a dynamic macromolecular “machine” responsible for removing introns and splicing together exons from eukaryotic precursor-mRNA transcripts
These U snRNPs assemble onto specific regions of the pre-mRNA and participate through different states of the splicing cycle [1] (Figure 1A)
A U1 snRNA variant used for crystallization had a truncated U1-SLII capped with a kissing loop motif that has only two cross-strand Watson-Crick GC base pair between two RNA molecules (2KL) [7,30] (Figure 5B)
Summary
Adelaine Kwun-Wai Leung 1, * , Yasushi Kondo 2,3 , Daniel A.
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