Characterization of the TRBP domain required for Dicer interaction and function in RNA interference

@article{Daniels2008CharacterizationOT,
  title={Characterization of the TRBP domain required for Dicer interaction and function in RNA interference},
  author={Sylvanne M Daniels and Carlos E Melendez-Pe{\~n}a and Robert J Scarborough and A{\"i}cha Daher and Helen S Christensen and Mohamed El Far and Damian Purcell and S{\'e}bastien Lain{\'e} and Anne Gatignol},
  journal={BMC Molecular Biology},
  year={2008},
  volume={10},
  pages={38 - 38}
}
Dicer, Ago2 and TRBP are the minimum components of the human RNA-induced silencing complex (RISC). While Dicer and Ago2 are RNases, TRBP is the double-stranded RNA binding protein (dsRBP) that loads small interfering RNA into the RISC. TRBP binds directly to Dicer through its C-terminal domain. We show that the TRBP binding site in Dicer is a 165 amino acid (aa) region located between the ATPase and the helicase domains. The binding site in TRBP is a 69 aa domain, called C4, located at the C… CONTINUE READING
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