title: New currency for old rope: from coiled-coil assemblies to α-helical barrels.
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.
authors.affiliation: School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK. D.N.Woolfson@bristol.ac.uk
authors.forename: Derek N
authors.initials: DN
authors.lastname: Woolfson
authors.forename: Gail J
authors.initials: GJ
authors.lastname: Bartlett
authors.forename: Marc
authors.initials: M
authors.lastname: Bruning
authors.forename: Andrew R
authors.initials: AR
authors.lastname: Thomson
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D020449:Repetitive Sequences, Amino Acid
chemical_list: D011506:Proteins