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

Woolfson, D. N., Bartlett, G. J., Bruning, M. and Thomson, A. R. (2012) New currency for old rope: from coiled-coil assemblies to α-helical barrels. Current Opinion in Structural Biology, 22(4), pp. 432-441. (doi:10.1016/ (PMID:22445228)

Full text not currently available from Enlighten.


α-Helical coiled coils are ubiquitous protein–protein-interaction domains. They share a relatively straightforward sequence repeat, which directs the folding and assembly of amphipathic α-helices. The helices can combine in a number of oligomerisation 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.

Item Type:Articles
Additional Information:The authors thank the BBSRC and EPSRC of the UK for funding (grant numbers: BB/G008833/1 and EP/ J01430/1).
Glasgow Author(s) Enlighten ID:Thomson, Dr Drew
Authors: Woolfson, D. N., Bartlett, G. J., Bruning, M., and Thomson, A. R.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Current Opinion in Structural Biology
Published Online:23 March 2012

University Staff: Request a correction | Enlighten Editors: Update this record