Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs.

@article{Oruganti2005StructuralCO,
  title={Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs.},
  author={Sri vdya Oruganti and YanMing Zhang and Hong Hai Li},
  journal={Biochemical and biophysical research communications},
  year={2005},
  volume={333 2},
  pages={550-4}
}
Snu13p is a bifunctional yeast protein involved in both messenger RNA splicing as well as ribosomal RNA maturation. Snu13p initiates assembly of ribonucleoprotein particles by interacting with a conserved RNA motif called kink turn. Unlike its archaeal homolog, L7Ae, Snu13p displays differential specificity for functionally distinct kink turns. Thus, the structures of Snu13p at different functional states, including those alone and bound with RNAs, are required to understand how the protein… CONTINUE READING

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