Ontology highlight
ABSTRACT:
SUBMITTER: Rhys GG
PROVIDER: S-EPMC6175849 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Rhys Guto G GG Wood Christopher W CW Lang Eric J M EJM Mulholland Adrian J AJ Brady R Leo RL Thomson Andrew R AR Woolfson Derek N DN
Nature communications 20181008 1
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<sub>n</sub>) or dihedral (D<sub>n</sub>) 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 bu ...[more]