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@ARTICLE{Sachyani:207416,
      author       = {Sachyani, Dana and Dvir, Meidan and Strulovich, Roi and
                      Tria, Giancarlo and Tobelaim, William and Peretz, Asher and
                      Pongs, Olaf and Svergun, Dmitri and Attali, Bernard and
                      Hirsch, Joel A.},
      title        = {{S}tructural {B}asis of a {K}v7.1 {P}otassium {C}hannel
                      {G}ating {M}odule: {S}tudies of the {I}ntracellular
                      {C}-{T}erminal {D}omain in {C}omplex with {C}almodulin},
      journal      = {Structure},
      volume       = {22},
      number       = {11},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PUBDB-2015-01326},
      pages        = {1582 - 1594},
      year         = {2014},
      note         = {(c) Elsevier Ltd.},
      abstract     = {Kv7 channels tune neuronal and cardiomyocyte excitability.
                      In addition to the channel membrane domain, they also have a
                      unique intracellular C-terminal (CT) domain, bound
                      constitutively to calmodulin (CaM). This CT domain regulates
                      gating and tetramerization. We investigated the structure of
                      the membrane proximal CT module in complex with CaM by X-ray
                      crystallography. The results show how the CaM intimately
                      hugs a two-helical bundle, explaining many channelopathic
                      mutations. Structure-based mutagenesis of this module in the
                      context of concatemeric tetramer channels and functional
                      analysis along with in vitro data lead us to propose that
                      one CaM binds to one individual protomer, without
                      crosslinking subunits and that this configuration is
                      required for proper channel expression and function.
                      Molecular modeling of the CT/CaM complex in conjunction with
                      small-angle X-ray scattering suggests that the membrane
                      proximal region, having a rigid lever arm, is a critical
                      gating regulator.},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000344934300006},
      pubmed       = {pmid:25441029},
      doi          = {10.1016/j.str.2014.07.016},
      url          = {https://bib-pubdb1.desy.de/record/207416},
}