Structure of the human 26S proteasome at a resolution of 3.9 Å.

  title={Structure of the human 26S proteasome at a resolution of 3.9 {\AA}.},
  author={Andreas Schweitzer and Antje Aufderheide and Till Rudack and Florian Beck and G{\"u}nter Pfeifer and J{\"u}rgen M Plitzko and Eri Sakata and Klaus Schulten and Friedrich F{\"o}rster and Wolfgang Baumeister},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={113 28},
Protein degradation in eukaryotic cells is performed by the Ubiquitin-Proteasome System (UPS). The 26S proteasome holocomplex consists of a core particle (CP) that proteolytically degrades polyubiquitylated proteins, and a regulatory particle (RP) containing the AAA-ATPase module. This module controls access to the proteolytic chamber inside the CP and is surrounded by non-ATPase subunits (Rpns) that recognize substrates and deubiquitylate them before unfolding and degradation. The architecture… CONTINUE READING
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