Structural biology of the PCI-protein fold

AM Ellisdon, M Stewart - Bioarchitecture, 2012 - Taylor & Francis
Bioarchitecture, 2012Taylor & Francis
The PCI fold is based on a stack of α-helices topped with a winged-helix domain and is
found in a range of proteins that form central parts of large complexes such as the
proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex.
Recent structural determinations have given intriguing insight into how these folds function
both to facilitate the generation of larger proteinaceous assembles and also to interact
functionally with nucleic acids.
The PCI fold is based on a stack of α-helices topped with a winged-helix domain and is found in a range of proteins that form central parts of large complexes such as the proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex. Recent structural determinations have given intriguing insight into how these folds function both to facilitate the generation of larger proteinaceous assembles and also to interact functionally with nucleic acids.
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