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New currency for old rope: from coiled-coil assemblies to α-helical barrels.
- Source :
-
Current opinion in structural biology [Curr Opin Struct Biol] 2012 Aug; Vol. 22 (4), pp. 432-41. Date of Electronic Publication: 2012 Mar 23. - Publication Year :
- 2012
-
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.<br /> (Copyright © 2012 Elsevier Ltd. All rights reserved.)
Details
- Language :
- English
- ISSN :
- 1879-033X
- Volume :
- 22
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Current opinion in structural biology
- Publication Type :
- Academic Journal
- Accession number :
- 22445228
- Full Text :
- https://doi.org/10.1016/j.sbi.2012.03.002