Secondary structure of a KCNE cytoplasmic domain
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology
Life Sciences | Medicine and Health Sciences
Type I transmembrane KCNE peptides contain a conserved C-terminal cytoplasmic domain that abuts the transmembrane segment. In KCNE1, this region is required for modulation of KCNQ1 K(+) channels to afford the slowly activating cardiac I(Ks) current. We utilized alanine/leucine scanning to determine whether this region possesses any secondary structure and to identify the KCNE1 residues that face the KCNQ1 channel complex. Helical periodicity analysis of the mutation-induced perturbations in voltage activation and deactivation kinetics of KCNQ1-KCNE1 complexes defined that the KCNE1 C terminus is alpha-helical when split in half at a conserved proline residue. This helical rendering assigns all known long QT mutations in the KCNE1 C-terminal domain as protein facing. The identification of a secondary structure within the KCNE1 C-terminal domain provides a structural scaffold to map protein-protein interactions with the pore-forming KCNQ1 subunit as well as the cytoplasmic regulatory proteins anchored to KCNQ1-KCNE complexes.
DOI of Published Version
J Gen Physiol. 2006 Dec;128(6):721-9. Link to article on publisher's site
The Journal of general physiology
Rocheleau JM, Gage SD, Kobertz WR. (2006). Secondary structure of a KCNE cytoplasmic domain. GSBS Student Publications. https://doi.org/10.1085/jgp.200609657. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1016