Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch.

@article{Thore2008StructuralBO,
  title={Structural basis of thiamine pyrophosphate analogues binding to the eukaryotic riboswitch.},
  author={St{\'e}phane Thore and Christian Frick and Nenad Ban},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 26},
  pages={8116-7}
}
The thiamine pyrophosphate (TPP)-sensing riboswitch is the only riboswitch found in eukaryotes. In plants, TPP regulates its own production by binding to the 3' untranslated region of the mRNA encoding ThiC, a critical enzyme in thiamine biosynthesis, which promotes the formation of an unstable splicing variant. In order to better understand the molecular basis of TPP-analogue binding to the eukaryotic TPP-responsive riboswitch, we have determined the crystal structures of the Arabidopsis… CONTINUE READING

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