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Sm proteins were discovered nearly 20 years ago as a group of small antigenicproteins ($\approx$ 90-120 residues). Since then, an extensive amount ofbiochemical and genetic data have illuminated the crucial roles of theseproteins in forming ribonucleoprotein (RNP) complexes that are used in RNAprocessing, e.g., spliceosomal removal of introns from pre-mRNAs. Spliceosomesare large macromolecular machines that are comparable to ribosomes in size andcomplexity, and are composed of uridine-rich small nuclear RNPs (U snRNPs).Various sets of seven different Sm proteins form the cores of most snRNPs.Despite their importance, very little is known about the atomic-resolutionstructure of snRNPs or their Sm cores. As a first step towards ahigh-resolution image of snRNPs and their hierarchic assembly, we havedetermined the crystal structures of archaeal homologs of Sm proteins, which weterm Sm-like archaeal proteins (SmAPs).

The Structures, Functions, and Evolution of Sm-like Archaeal Proteins (SmAPs)