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@ARTICLE{Schnke:5102,
      author       = {Schünke, S. and Stoldt, M. and Novak, K. and Kaupp, U. B.
                      and Willbold, D.},
      title        = {{S}olution structure of the {M}esorhizobium loti {K}1
                      channel cyclic nucleotide-binding domain in complex with
                      c{AMP}},
      journal      = {EMBO reports},
      volume       = {10},
      issn         = {1469-221X},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {PreJuSER-5102},
      pages        = {729 - 735},
      year         = {2009},
      note         = {This study was supported by a research grant from the
                      Helmholtzgemeinschaft},
      abstract     = {Cyclic nucleotide-sensitive ion channels, known as HCN and
                      CNG channels, are crucial in neuronal excitability and
                      signal transduction of sensory cells. HCN and CNG channels
                      are activated by binding of cyclic nucleotides to their
                      intracellular cyclic nucleotide-binding domain (CNBD).
                      However, the mechanism by which the binding of cyclic
                      nucleotides opens these channels is not well understood.
                      Here, we report the solution structure of the isolated CNBD
                      of a cyclic nucleotide-sensitive K(+) channel from
                      Mesorhizobium loti. The protein consists of a wide
                      anti-parallel beta-roll topped by a helical bundle
                      comprising five alpha-helices and a short 3(10)-helix. In
                      contrast to the dimeric arrangement ('dimer-of-dimers') in
                      the crystal structure, the solution structure clearly shows
                      a monomeric fold. The monomeric structure of the CNBD
                      supports the hypothesis that the CNBDs transmit the binding
                      signal to the channel pore independently of each other.},
      keywords     = {Alphaproteobacteria: chemistry / Crystallography, X-Ray /
                      Cyclic AMP: chemistry / Cyclic AMP: metabolism / Cyclic
                      Nucleotide-Gated Cation Channels: chemistry / Cyclic
                      Nucleotide-Gated Cation Channels: metabolism / Models,
                      Molecular / Potassium Channels: chemistry / Potassium
                      Channels: metabolism / Protein Structure, Secondary /
                      Protein Structure, Tertiary / Solutions / Cyclic
                      Nucleotide-Gated Cation Channels (NLM Chemicals) / Potassium
                      Channels (NLM Chemicals) / Solutions (NLM Chemicals) /
                      Cyclic AMP (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-1 / ISB-3 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB922 / I:(DE-Juel1)VDB942 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {Programm Biosoft / Funktion und Dysfunktion des
                      Nervensystems},
      pid          = {G:(DE-Juel1)FUEK443 / G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19465888},
      pmc          = {pmc:PMC2727438},
      UT           = {WOS:000267599700015},
      doi          = {10.1038/embor.2009.68},
      url          = {https://juser.fz-juelich.de/record/5102},
}