Structural basis of m(7)GpppG binding to poly(A)-specific ribonuclease.

  title={Structural basis of m(7)GpppG binding to poly(A)-specific ribonuclease.},
  author={Mousheng Wu and Per Eric Nilsson and Niklas Henriksson and Anna Niedzwiecka and Meng Kiat Lim and Zhihong Cheng and Kyriakos Kokkoris and Anders Virtanen and Haiwei Song},
  volume={17 2},
Poly(A)-specific ribonuclease (PARN) is a homodimeric, processive, and cap-interacting 3' exoribonuclease that efficiently degrades eukaryotic mRNA poly(A) tails. The crystal structure of a C-terminally truncated PARN in complex with m(7)GpppG reveals that, in one subunit, m(7)GpppG binds to a cavity formed by the RRM domain and the nuclease domain, whereas in the other subunit, it binds almost exclusively to the RRM domain. Importantly, our structural and competition data show that the cap… CONTINUE READING

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