The structure of the CstF-77 homodimer provides insights into CstF assembly

@inproceedings{Legrand2007TheSO,
  title={The structure of the CstF-77 homodimer provides insights into CstF assembly},
  author={Pierre François Legrand and No{\"e}l Pinaud and Lionel Minvielle-S{\'e}bastia and S{\'e}bastien Fribourg},
  booktitle={Nucleic acids research},
  year={2007}
}
The cleavage stimulation factor (CstF) is essential for the first step of poly(A) tail formation at the 3' ends of mRNAs. This heterotrimeric complex is built around the 77-kDa protein bridging both CstF-64 and CstF-50 subunits. We have solved the crystal structure of the 77-kDa protein from Encephalitozoon cuniculi at a resolution of 2 A. The structure folds around 11 Half-a-TPR repeats defining two domains. The crystal structure reveals a tight homodimer exposing phylogenetically conserved… CONTINUE READING

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