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@ARTICLE{DosSantosMorais:856718,
      author       = {Dos Santos Morais, Raphael and Delalande, Olivier and
                      Pérez, Javier and Mias-Lucquin, Dominique and Lagarrigue,
                      Mélanie and Martel, Anne and Molza, Anne-Elisabeth and
                      Chéron, Angélique and Raguénès-Nicol, Céline and
                      Chenuel, Thomas and Bondon, Arnaud and Appavou, Marie-Sousai
                      and Le Rumeur, Elisabeth and Combet, Sophie and Hubert,
                      Jean-François},
      title        = {{H}uman {D}ystrophin {S}tructural {C}hanges upon {B}inding
                      to {A}nionic {M}embrane {L}ipids},
      journal      = {Biophysical journal},
      volume       = {115},
      number       = {7},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-06069},
      pages        = {1231 - 1239},
      year         = {2018},
      abstract     = {Scaffolding proteins play important roles in supporting the
                      plasma membrane (sarcolemma) of muscle cells.Among them,
                      dystrophin strengthens the sarcolemma through protein-lipid
                      interactions, and its absence due to gene mutationsleads to
                      the severe Duchenne muscular dystrophy. Most of the
                      dystrophin protein consists of a central domain made of 24
                      spec-trin-like coiled-coil repeats (R). Using small angle
                      neutron scattering (SANS) and the contrast variation
                      technique, we specificallyprobed the structure of the three
                      first consecutive repeats 1–3 (R1–3), a part of
                      dystrophin known to physiologically interact withmembrane
                      lipids. R1–3 free in solution was compared to its
                      structure adopted in the presence of phospholipid-based
                      bicelles.SANS data for the protein/lipid complexes were
                      obtained with contrast-matched bicelles under various
                      phospholipid composi-tions to probe the role of
                      electrostatic interactions. When bound to anionic bicelles,
                      large modifications of the protein three-dimensional
                      structure were detected, as revealed by a significant
                      increase of the protein gyration radius from 42 51 to60 54
                      A˚. R1–3/anionic bicelle complexes were further analyzed
                      by coarse-grained molecular dynamics simulations. Fromthese
                      studies, we report an all-atom model of R1–3 that
                      highlights the opening of the R1 coiled-coil repeat when
                      bound tothe membrane lipids. This model is totally in
                      agreement with SANS and click chemistry/mass spectrometry
                      data. We concludethat the sarcolemma membrane anchoring that
                      occurs during the contraction/elongation process of muscles
                      could be ensuredby this coiled-coil opening. Therefore,
                      understanding these structural changes may help in the
                      design of rationalized shorteneddystrophins for gene
                      therapy. Finally, our strategy opens up new possibilities
                      for structure determination of peripheral and inte-gral
                      membrane proteins not compatible with different
                      high-resolution structural methods.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101 / EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30197181},
      UT           = {WOS:000446056300010},
      doi          = {10.1016/j.bpj.2018.07.039},
      url          = {https://juser.fz-juelich.de/record/856718},
}