New currency for old rope: from coiled-coil assemblies to alpha-helical barrels

Derek N. Woolfson*, Gail J. Bartlett, Marc Bruning, A R Thomson

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

97 Citations (Scopus)

Abstract

alpha-Helical coiled coils are ubiquitous protein-protein-interaction domains. They share a relatively straightforward sequence repeat, which directs the folding and assembly of amphipathic helices. The helices can combine in a number of oligonnerisation states and topologies to direct a wide variety of protein assemblies. Although in nature parallel dimers, trimers and tetramers dominate, the potential to form larger oligomers and more-complex assemblies has long been recognised. In particular, complexes above pentamer are interesting because they are barrel-like, having central channels or pores with well-defined dimensions and chemistry. Recent empirical and rational design experiments are beginning to chart this potential new territory in coiled-coil space, leading to intriguing new structures, and possibilities for functionalisation and applications.

Original languageEnglish
Pages (from-to)432-441
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume22
Issue number4
DOIs
Publication statusPublished - Aug 2012

Structured keywords

  • Bristol BioDesign Institute

Keywords

  • GCN4 LEUCINE-ZIPPER
  • BURIED POLAR RESIDUES
  • CRYSTAL-STRUCTURE
  • MECHANOSENSITIVE CHANNEL
  • ANGSTROM RESOLUTION
  • PROTEIN STRUCTURES
  • SYNTHETIC BIOLOGY
  • MEMBRANE-PROTEIN
  • PACKING
  • DESIGN

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