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@ARTICLE{Kowal:153358,
      author       = {Kowal, Julia and Chami, Mohamed and Baumgartner, Paul and
                      Arheit, Marcel and Chiu, Po-Lin and Rangl, Martina and
                      Scheuring, Simon and Schröder, Gunnar F. and Nimigean,
                      Crina M. and Stahlberg, Henning},
      title        = {{L}igand-induced structural changes in the cyclic
                      nucleotide-modulated potassium channel {M}lo{K}1},
      journal      = {Nature Communications},
      volume       = {5},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2014-02989},
      pages        = {(1-10) 4106},
      year         = {2014},
      abstract     = {Cyclic nucleotide-modulated ion channels are important for
                      signal transduction and pacemaking in eukaryotes. The
                      molecular determinants of ligand gating in these channels
                      are still unknown, mainly because of a lack of direct
                      structural information. Here we report ligand-induced
                      conformational changes in full-length MloK1, a cyclic
                      nucleotide-modulated potassium channel from the bacterium
                      Mesorhizobium loti, analysed by electron crystallography and
                      atomic force microscopy. Upon cAMP binding, the cyclic
                      nucleotide-binding domains move vertically towards the
                      membrane, and directly contact the S1–S4 voltage sensor
                      domains. This is accompanied by a significant shift and tilt
                      of the voltage sensor domain helices. In both states, the
                      inner pore-lining helices are in an ‘open’ conformation.
                      We propose a mechanism in which ligand binding can favour
                      pore opening via a direct interaction between the cyclic
                      nucleotide-binding domains and voltage sensors. This offers
                      a simple mechanistic hypothesis for the coupling between
                      ligand gating and voltage sensing in eukaryotic HCN
                      channels.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000331084400015},
      pubmed       = {pmid:24469021},
      doi          = {10.1038/ncomms4106},
      url          = {https://juser.fz-juelich.de/record/153358},
}