Inherent protein structural flexibility at the RNA-binding interface of L30e.

@article{Chao2003InherentPS,
  title={Inherent protein structural flexibility at the RNA-binding interface of L30e.},
  author={Jeffrey A Chao and Gandham S. Prasad and Susan A. White and Charles David Stout and James R Williamson},
  journal={Journal of molecular biology},
  year={2003},
  volume={326 4},
  pages={999-1004}
}
The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined. The flexible RNA-binding region in the L30… CONTINUE READING