Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins.

@article{Christie2013StructureOT,
  title={Structure of the PAN3 pseudokinase reveals the basis for interactions with the PAN2 deadenylase and the GW182 proteins.},
  author={Mary Christie and Andreas Boland and Eric Huntzinger and Oliver Weichenrieder and Elisa Izaurralde},
  journal={Molecular cell},
  year={2013},
  volume={51 3},
  pages={
          360-73
        }
}
  • Mary Christie, Andreas Boland, +2 authors Elisa Izaurralde
  • Published 2013
  • Medicine, Biology
  • Molecular cell
  • The PAN2-PAN3 deadenylase complex functions in general and miRNA-mediated mRNA degradation and is specifically recruited to miRNA targets by GW182/TNRC6 proteins. We describe the PAN3 adaptor protein crystal structure that, unexpectedly, forms intertwined and asymmetric homodimers. Dimerization is mediated by a coiled coil that links an N-terminal pseudokinase to a C-terminal knob domain. The PAN3 pseudokinase binds ATP, and this function is required for mRNA degradation in vivo. We further… CONTINUE READING

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