Structural biology of the PCI-protein fold

Bioarchitecture. 2012 Jul-Aug;2(4):118-23. doi: 10.4161/bioa.21131. Epub 2012 Jul 1.

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.

Keywords: COP9 complex; PCI fold; PCI protein; TREX-2 complex; eIF3; proteasome.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Models, Molecular
  • Nucleic Acids / chemistry
  • Nucleic Acids / metabolism
  • Proteasome Endopeptidase Complex / metabolism
  • Protein C Inhibitor / chemistry*
  • Protein C Inhibitor / metabolism*
  • Protein Folding*
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • Nucleic Acids
  • Protein C Inhibitor
  • SEM1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Proteasome Endopeptidase Complex