title: Structural biology of the PCI-protein fold.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology; Monash University; Clayton, Victoria, Australia.
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Ellisdon
authors.affiliation: MRC Laboratory of Molecular Biology; Cambridge, UK.
authors.forename: Murray
authors.initials: M
authors.lastname: Stewart
mesh_terms: D006801:Humans; D008958:Models, Molecular; D009696:Nucleic Acids / Q000737:chemistry / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D018046:Protein C Inhibitor / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism
chemical_list: D009696:Nucleic Acids; D018046:Protein C Inhibitor; C117424:SEM1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D046988:Proteasome Endopeptidase Complex