Functional and structural characterization of interactions between opposite subunits in HCN pacemaker channels
M. Kondapuram, B. Frieg, S. Yueksel, T. Schwabe, C. Sattler, M. Lelle, A. Schweinitz, R. Schmauder, K. Benndorf, H. Gohlke, J. Kusch
The paper identifies residue K464 in the C-linker of HCN2 channels as critical for stabilizing the closed state through interactions with opposite subunits, supported by mutagenesis, electrophysiology, and molecular dynamics simulations.
bioRxiv · Sep 21, 2020Biophysics