% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Kondapuram:890666,
      author       = {Kondapuram, Mahesh and Frieg, Benedikt and Yüksel, Sezin
                      and Schwabe, Tina and Sattler, Christian and Lelle, Marco
                      and Schweinitz, Andrea and Schmauder, Ralf and Benndorf,
                      Klaus and Gohlke, Holger and Kusch, Jana},
      title        = {{F}unctional and structural characterization of
                      interactions between opposite subunits in {HCN} pacemaker
                      channels},
      journal      = {bioRxiv beta},
      address      = {Cold Spring Harbor},
      publisher    = {Cold Spring Harbor Laboratory, NY},
      reportid     = {FZJ-2021-01114},
      year         = {2020},
      abstract     = {Hyperpolarization-activated and cyclic nucleotide (HCN)
                      modulated channels are tetrameric cation channels. In each
                      of the four subunits, the intracellular cyclic
                      nucleotide-binding domain (CNBD) is coupled to the
                      transmembrane domain via a helical structure, the C-linker.
                      High-resolution channel structures suggest that the C-linker
                      enables functionally relevant interactions with the opposite
                      subunit, which might be critical for coupling the
                      conformational changes in the CNBD to the channel pore. We
                      combined mutagenesis, patch-clamp technique, confocal
                      patch-clamp fluorometry, and molecular dynamics simulations
                      to show that residue K464 of the C-linker is essential for
                      stabilizing the closed state of the mHCN2 channel by forming
                      interactions with the opposite subunit. MD simulations
                      revealed that both cAMP and K464E induce a rotation of the
                      intracellular domain relative to the channel pore, weakening
                      the autoinhibitory effect of the unoccupied CL-CNBD region.
                      The adopted poses are in excellent agreement with structural
                      results.},
      ddc          = {570},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1101/2020.09.21.305797},
      url          = {https://juser.fz-juelich.de/record/890666},
}