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@ARTICLE{Kondapuram:907779,
      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      = {Communications biology},
      volume       = {5},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2022-02208},
      pages        = {430},
      year         = {2022},
      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 (MD)
                      simulations to show that residue K464 of the C-linker is
                      relevant for stabilizing the closed state of the mHCN2
                      channel by forming interactions with the opposite subunit.
                      MD simulations revealed that in the K464E channel, a
                      rotation of the intracellular domain relative to the channel
                      pore is induced, which is similar to the cAMP-induced
                      rotation, weakening the autoinhibitory effect of the
                      unoccupied CL-CNBD region. We suggest that this CL-CNBD
                      rotation is considerably involved in activation-induced
                      affinity increase but only indirectly involved in gate
                      modulation. The adopted poses shown herein are in excellent
                      agreement with previous structural results.},
      cin          = {IBG-4 / JSC / NIC / IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      Forschergruppe Gohlke $(hkf7_20200501)$ / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      $G:(DE-Juel1)hkf7_20200501$ / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35534535},
      UT           = {WOS:000792648600004},
      doi          = {10.1038/s42003-022-03360-6},
      url          = {https://juser.fz-juelich.de/record/907779},
}