The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α

@article{Jinek2004TheST,
  title={The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α},
  author={Martin Jinek and Jan Rehwinkel and Brooke D Lazarus and Elisa Izaurralde and John A Hanover and Elena Conti},
  journal={Nature Structural &Molecular Biology},
  year={2004},
  volume={11},
  pages={1001-1007}
}
Addition of N-acetylglucosamine (GlcNAc) is a ubiquitous form of intracellular glycosylation catalyzed by the conserved O-linked GlcNAc transferase (OGT). OGT contains an N-terminal domain of tetratricopeptide (TPR) repeats that mediates the recognition of a broad range of target proteins. Components of the nuclear pore complex are major OGT targets, as OGT depletion by RNA interference (RNAi) results in the loss of GlcNAc modification at the nuclear envelope. To gain insight into the mechanism… CONTINUE READING
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