% 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{Pfleger:890419,
      author       = {Pfleger, Christopher and Kusch, Jana and Kondapuram, Mahesh
                      and Schwabe, Tina and Sattler, Christian and Benndorf, Klaus
                      and Gohlke, Holger},
      title        = {{A}llosteric signaling in {C}-linker and cyclic
                      nucleotide-binding domain of {HCN}2 channels},
      journal      = {Biophysical journal},
      volume       = {120},
      number       = {5},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-00939},
      pages        = {950-963},
      year         = {2021},
      abstract     = {Opening of hyperpolarization-activated cyclic
                      nucleotide-modulated (HCN) channels is controlled by
                      membrane hyperpolarization and binding of cyclic nucleotides
                      to the tetrameric cyclic nucleotide-binding domain (CNBD),
                      attached to the C-linker disk (CL). Confocal patch-clamp
                      fluorometry revealed pronounced cooperativity of ligand
                      binding among protomers. However, by which pathways
                      allosteric signal transmission occurs remained elusive.
                      Here, we investigate how changes in the structural dynamics
                      of the CL-CNBD of mouse HCN2 upon cAMP binding relate to
                      inter- and intrasubunit signal transmission. Applying a
                      rigidity theory-based approach, we identify two intersubunit
                      and one intrasubunit pathways that differ in allosteric
                      coupling strength between cAMP binding sites or towards the
                      CL. These predictions agree with results from
                      electrophysiological and patch-clamp fluorometry
                      experiments. Our results map out distinct routes within the
                      CL-CNBD that modulate different cAMP binding responses in
                      HCN2 channels. They signify that functionally relevant
                      submodules may exist within and across structurally
                      discernable subunits in HCN channels.},
      cin          = {JSC / NIC / IBI-7},
      ddc          = {570},
      cid          = {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) / Forschergruppe
                      Gohlke $(hkf7_20200501)$},
      pid          = {G:(DE-HGF)POF4-5111 / $G:(DE-Juel1)hkf7_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33515603},
      UT           = {WOS:000630953600021},
      doi          = {10.1016/j.bpj.2021.01.017},
      url          = {https://juser.fz-juelich.de/record/890419},
}