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/j.sbi.2012.03.002) (PMID:22445228)
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Abstract
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 |
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Additional Information: | The authors thank the BBSRC and EPSRC of the UK for funding (grant numbers: BB/G008833/1 and EP/ J01430/1). |
Status: | Published |
Refereed: | Yes |
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 |
Publisher: | Elsevier |
ISSN: | 0959-440X |
Published Online: | 23 March 2012 |
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