Biochemical Society Transactions · 2001 · 42 citations · 5 references
Life SciencesBiologyMolecular BiologyRna ProcessingStructural BiologyStructural BiophysicsIntron StructureProtein StructureRna SplicingRna StructureRna-protein InteractionsSmall Nuclear Rna BiologyProtein ComplexesRna-protein ComplexesSpliceosome AssemblySpliceosome ComplexesU2 Small Nuclear RnaU5 Small Nuclear RibonucleoproteinU5 Small Nuclear RnaU6.u5 Small Nuclear Ribonucleoprotein
The spliceosome is a macromolecular machine that carries out the excision of introns from eukaryotic pre-mRNAs and splicing together of exons. Four large RNA-protein complexes, called the U1, U2, U4/U6 and U5 small nuclear ribo-nucleoprotein particles (snRNPs), and some non-snRNP proteins assemble around three short conserved sequences within the intron in an ordered manner to form the active spliceosome. We aim to provide insight into the molecular details of the mechanism of pre-mRNA splicing through crystallographic studies of the snRNPs. We have solved the X-ray crystal structure of some snRNP proteins as part of either protein-protein complexes or RNA-protein complexes. These structures have provided an important insight into the overall architecture of the U1 and U2 snRNPs and the mechanisms of RNA-protein and protein-protein recognition.
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Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
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