Maintaining and breaking symmetry in homomeric coiled-coil assemblies.

ABSTRACT: In coiled-coil (CC) protein structures α-helices wrap around one another to form rope-like assemblies. Most natural and designed CCs have two-four helices and cyclic (C_n) or dihedral (D_n) symmetry. Increasingly, CCs with five or more helices are being reported. A subset of these higher-order CCs is of interest as they have accessible central channels that can be functionalised; they are α-helical barrels. These extended cavities are surprising given the drive to maximise buried hydrophobic surfaces during protein folding and assembly in water. Here, we show that α-helical barrels can be maintained by the strategic placement of β-branched aliphatic residues lining the lumen. Otherwise, the structures collapse or adjust to give more-complex multi-helix assemblies withou

SUBMITTER: Rhys GG 

PROVIDER: S-EPMC6175849 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature