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@ARTICLE{Schnke:11494,
      author       = {Schünke, S. and Lecher, J. and Stoldt, M. and Kaupp, U. B.
                      and Willbold, D.},
      title        = {{R}esonance assignments of the nucleotide-free wildtype
                      {M}lo{K}1 cyclic nucleotide-binding domain},
      journal      = {Biomolecular NMR assignments},
      volume       = {4},
      issn         = {1874-2718},
      address      = {Dordrecht [u.a.]},
      publisher    = {Springer Netherlands},
      reportid     = {PreJuSER-11494},
      pages        = {147 - 150},
      year         = {2010},
      note         = {This work was supported by a fellowship from the
                      International Research School "BioStruct'' to S. Schunke and
                      a research grant from the Helmholtz-Gemeinschaft ("Virtual
                      Institute of Structural Biology'') to D. Willbold.},
      abstract     = {Cyclic nucleotide-sensitive ion channels, known as HCN and
                      CNG channels play crucial roles in neuronal excitability and
                      signal transduction of sensory cells. These channels are
                      activated by binding of cyclic nucleotides to their
                      intracellular cyclic nucleotide-binding domain (CNBD). A
                      comparison of the structures of wildtype ligand-free and
                      ligand-bound CNBD is essential to elucidate the mechanism
                      underlying nucleotide-dependent activation of CNBDs. We
                      recently reported the solution structure of the
                      Mesorhizobium loti K1 (MloK1) channel CNBD in complex with
                      cAMP. We have now extended these studies and achieved nearly
                      complete assignments of (1)H, (13)C and (15)N resonances of
                      the nucleotide-free CNBD. A completely new assignment of the
                      nucleotide-free wildtype CNBD was necessary due to the
                      sizable chemical shift differences as compared to the cAMP
                      bound CNBD and the slow exchange behaviour between both
                      forms. Scattering of these chemical shift differences over
                      the complete CNBD suggests that nucleotide binding induces
                      significant overall conformational changes.},
      keywords     = {Cyclic Nucleotide-Gated Cation Channels: chemistry /
                      Nuclear Magnetic Resonance, Biomolecular / Nucleotides:
                      metabolism / Protein Structure, Tertiary / Rhizobium:
                      metabolism / Cyclic Nucleotide-Gated Cation Channels (NLM
                      Chemicals) / Nucleotides (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biophysics / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20449776},
      UT           = {WOS:000282317100007},
      doi          = {10.1007/s12104-010-9231-z},
      url          = {https://juser.fz-juelich.de/record/11494},
}