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@ARTICLE{Song:293456,
      author       = {Song, Jae-Geun and Kostan, Julius and Drepper, Friedel and
                      Knapp, Bettina and de Almeida Ribeiro, Euripedes and
                      Konarev, Petr V. and Grishkovskaya, Irina and Wiche,
                      Gerhard and Gregor, Martin and Svergun, Dmitri I. and
                      Warscheid, Bettina and Djinović-Carugo, Kristina},
      title        = {{S}tructural {I}nsights into
                      $\mathrm{{C}a^{2+}}$-{C}almodulin {R}egulation of {P}lectin
                      1a-{I}ntegrin β4 {I}nteraction in {H}emidesmosomes},
      journal      = {Structure},
      volume       = {23},
      number       = {3},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PUBDB-2016-00545},
      pages        = {558 - 570},
      year         = {2015},
      abstract     = {The mechanical stability of epithelial cells, whichprotect
                      organisms from harmful external factors, ismaintained by
                      hemidesmosomes via the interactionbetween plectin 1a (P1a)
                      and integrin a6b4. Bindingof calcium-calmodulin (Ca 2+ -CaM)
                      to P1a togetherwith phosphorylation of integrin b4 disrupts
                      thiscomplex, resulting in disassembly of hemidesmo-somes. We
                      present structures of the P1a actin bind-ing domain either
                      in complex with the N-ter lobe ofCa 2+ -CaM or with the
                      first pair of integrin b4 fibro-nectin domains. Ca 2+ -CaM
                      binds to the N-ter iso-form-specific tail of P1a in a unique
                      manner, via itsN-ter lobe in an extended conformation.
                      Structural,cell biology, and biochemical studies suggest
                      thefollowing model: binding of Ca 2+ -CaM to an
                      intrinsi-cally disordered N-ter segment of plectin
                      convertsit to an a helix, which repositions calmodulin
                      todisplace integrin b4 by steric repulsion. This modelcould
                      serve as a blueprint for studies aimed at under-standing how
                      Ca 2+ -CaM or EF-hand motifs regulateF-actin-based
                      cytoskeleton.},
      cin          = {EMBL / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {899 - ohne Topic (POF3-899) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570)},
      pid          = {G:(DE-HGF)POF3-899 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000350886100014},
      pubmed       = {pmid:25703379},
      doi          = {10.1016/j.str.2015.01.011},
      url          = {https://bib-pubdb1.desy.de/record/293456},
}