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@ARTICLE{Schnke:16576,
      author       = {Schünke, S. and Stoldt, M. and Lecher, J. and Kaupp, U.B.
                      and Willbold, D.},
      title        = {{S}tructural insights into conformational changes of a
                      cyclic nucleotide-binding domain in solution from
                      {M}esorhizobium loti {K}1 channel},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {108},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PreJuSER-16576},
      pages        = {6121 - 6126},
      year         = {2011},
      note         = {This study was supported by a fellowship from the
                      International Research School BioStruct to S.S. and a
                      research grant from the Helmholtz-Gemeinschaft (Virtual
                      Institute of Structural Biology) to D.W.},
      abstract     = {Cyclic nucleotide-sensitive ion channels, known as HCN and
                      CNG channels, are activated by binding of ligands to a
                      domain (CNBD) located on the cytoplasmic side of the
                      channel. The underlying mechanisms are not well understood.
                      To elucidate the gating mechanism, structures of both the
                      ligand-free and -bound CNBD are required. Several crystal
                      structures of the CNBD from HCN2 and a bacterial CNG channel
                      (MloK1) have been solved. However, for HCN2, the cAMP-free
                      and -bound state did not reveal substantial structural
                      rearrangements. For MloK1, structural information for the
                      cAMP-free state has only been gained from mutant CNBDs.
                      Moreover, in the crystal, the CNBD molecules form an
                      interface between dimers, proposed to be important for
                      allosteric channel gating. Here, we have determined the
                      solution structure by NMR spectroscopy of the cAMP-free
                      wild-type CNBD of MloK1. A comparison of the solution
                      structure of cAMP-free and -bound states reveals large
                      conformational rearrangement on ligand binding. The two
                      structures provide insights on a unique set of
                      conformational events that accompany gating within the
                      ligand-binding site.},
      keywords     = {Alphaproteobacteria: metabolism / Crystallography, X-Ray /
                      Cyclic AMP: chemistry / Cyclic Nucleotide-Gated Cation
                      Channels: chemistry / Cyclic Nucleotide-Gated Cation
                      Channels: genetics / Mutation / Nuclear Magnetic Resonance,
                      Biomolecular / Protein Structure, Tertiary / Cyclic
                      Nucleotide-Gated Cation Channels (NLM Chemicals) / Cyclic
                      AMP (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Multidisciplinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21430265},
      pmc          = {pmc:PMC3076860},
      UT           = {WOS:000289413600042},
      doi          = {10.1073/pnas.1015890108},
      url          = {https://juser.fz-juelich.de/record/16576},
}