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@ARTICLE{Fahrenkamp:827850,
      author       = {Fahrenkamp, Dirk and Li, Jinyu and Ernst, Sabrina and
                      Schmitz-Van de Leur, Hildegard and Chatain, Nicolas and
                      Küster, Andrea and Koschmieder, Steffen and Lüscher,
                      Bernhard and Rossetti, Giulia and Müller-Newen, Gerhard},
      title        = {{I}ntramolecular hydrophobic interactions are critical
                      mediators of {STAT}5 dimerization},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-01941},
      pages        = {35454 -},
      year         = {2016},
      abstract     = {STAT5 is an essential transcription factor in
                      hematopoiesis, which is activated through tyrosine
                      phosphorylation in response to cytokine stimulation.
                      Constitutive activation of STAT5 is a hallmark of myeloid
                      and lymphoblastic leukemia. Using homology modeling and
                      molecular dynamics simulations, a model of the STAT5
                      phosphotyrosine-SH2 domain interface was generated providing
                      first structural information on the activated STAT5 dimer
                      including a sequence, for which no structural information is
                      available for any of the STAT proteins. We identified a
                      novel intramolecular interaction mediated through F706,
                      adjacent to the phosphotyrosine motif, and a unique
                      hydrophobic interface on the surface of the SH2 domain.
                      Analysis of corresponding STAT5 mutants revealed that this
                      interaction is dispensable for Epo receptor-mediated
                      phosphorylation of STAT5 but essential for dimer formation
                      and subsequent nuclear accumulation. Moreover, the herein
                      presented model clarifies molecular mechanisms of recently
                      discovered leukemic STAT5 mutants and will help to guide
                      future drug development.},
      cin          = {JSC / IAS-5 / INM-9},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)INM-9-20140121},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000385586200001},
      doi          = {10.1038/srep35454},
      url          = {https://juser.fz-juelich.de/record/827850},
}