Abstract
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.
Acknowledgments
We are most grateful to our colleagues in Melbourne and Cambridge for the helpful comments and suggestions. Supported in part by Medical Research Council Grant U105178939 (M.S.) and a Wellcome Trust Programme grant (M.S.). AME held EMBO and Marie Curie Postdoctoral fellowships.