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@ARTICLE{Premchandar:127320,
      author       = {A. Premchandar and A. Kupniewska and K. Tarnowski and N.
                      Mücke$^*$ and M. Mauermann$^*$ and M. Kaus-Drobek and A.
                      Edelman and H. Herrmann$^*$ and M. Dadlez},
      title        = {{A}nalysis of distinct molecular assembly complexes of
                      keratin {K}8 and {K}18 by hydrogen-deuterium exchange.},
      journal      = {Journal of structural biology},
      volume       = {192},
      number       = {3},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2017-03345},
      pages        = {426 - 440},
      year         = {2015},
      abstract     = {Keratins are intermediate filament (IF) proteins that form
                      complex filament systems in epithelial cells, thus serving
                      as scaffolding elements and mechanical stress absorbers. The
                      building blocks of keratin IFs are parallel coiled-coil
                      dimers of two distinct sequence-related proteins
                      distinguished as type I and type II keratins. To gain more
                      insight into their structural dynamics, we resorted to
                      hydrogen-deuterium exchange mass spectrometry of keratins K8
                      and K18, which are characteristic for simple epithelial
                      cells. Using this powerful technique not employed with IFs
                      before, we mapped patterns of protected versus unprotected
                      regions in keratin complexes at various assembly levels. In
                      particular, we localized protein segments exhibiting
                      different hydrogen exchange patterns in tetramers versus
                      filaments. We observed a general pattern of precisely
                      positioned regions of stability intertwining with flexible
                      regions, mostly represented by the non-α-helical segments.
                      Notably, some regions within the coiled-coil domains are
                      significantly more dynamic than others, while the
                      IF-consensus motifs at the end domains of the central
                      α-helical 'rod' segment, which mediate the 'head-to-tail'
                      dimer-dimer interaction in the filament elongation process,
                      become distinctly more protected upon formation of
                      filaments. Moreover, to gain more insight into the dynamics
                      of the individual keratins, we investigated the properties
                      of homomeric preparations of K8 and K18. The physiological
                      importance of keratins without a partner is encountered in
                      both pathological and experimental situations when one of
                      the two species is present in robust excess or completely
                      absent, such as in gene-targeted mice.},
      keywords     = {Keratins (NLM Chemicals)},
      cin          = {B065 / B040},
      ddc          = {540},
      cid          = {I:(DE-He78)B065-20160331 / I:(DE-He78)B040-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26434626},
      doi          = {10.1016/j.jsb.2015.10.001},
      url          = {https://inrepo02.dkfz.de/record/127320},
}