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@ARTICLE{Schumann:1021663,
      author       = {Schumann, Wibke and Loschwitz, Jennifer and Reiners, Jens
                      and Degrandi, Daniel and Legewie, Larissa and Stühler, Kai
                      and Pfeffer, Klaus and Poschmann, Gereon and Smits, Sander
                      H. J. and Strodel, Birgit},
      title        = {{I}ntegrative modeling of guanylate binding protein dimers},
      journal      = {Protein science},
      volume       = {32},
      number       = {12},
      issn         = {0961-8368},
      address      = {Bethesda, Md.},
      publisher    = {Protein Society},
      reportid     = {FZJ-2024-00919},
      pages        = {e4818},
      year         = {2023},
      abstract     = {Guanylate-binding proteins (GBPs) are essential
                      interferon-γ-activated largeGTPases that play a crucial
                      role in host defense against intracellular bacteriaand
                      parasites. While their protective functions rely on protein
                      polymerization,our understanding of the structural
                      intricacies of these multimerized statesremains limited. To
                      bridge this knowledge gap, we present dimer models forhuman
                      GBP1 (hGBP1) and murine GBP2 and 7 (mGBP2 and mGBP7) usingan
                      integrative approach, incorporating the crystal structure of
                      hGBP1's GTPasedomain dimer, crosslinking mass spectrometry,
                      small-angle X-ray scattering,protein–protein docking, and
                      molecular dynamics simulations. Our investiga-tion begins by
                      comparing the protein dynamics of hGBP1, mGBP2, andmGBP7. We
                      observe that the M/E domain in all three proteins exhibits
                      signifi-cant mobility and hinge motion, with mGBP7
                      displaying a slightly less pro-nounced motion but greater
                      flexibility in its GTPase domain. These dynamicdistinctions
                      can be attributed to variations in the sequences of mGBP7
                      andhGBP1/mGBP2, resulting in different dimerization modes.
                      Unlike hGBP1 andits close ortholog mGBP2, which exclusively
                      dimerize through their GTPasedomains, we find that mGBP7
                      exhibits three equally probable alternativedimer structures.
                      The GTPase domain of mGBP7 is only partially involved inits
                      dimerization, primarily due to an accumulation of negative
                      charge, allowingmGBP7 to dimerize independently of GTP.
                      Instead, mGBP7 exhibits a strong tendency to dimerize in an
                      antiparallel arrangement across its stalks. Theresults of
                      this work go beyond the sequence–structure–function
                      relationship,as the sequence differences in mGBP7 and
                      mGBP2/hGBP1 do not lead to dif-ferent structures, but to
                      different protein dynamics and dimerization. The dis-tinct
                      GBP dimer structures are expected to encode specific
                      functions crucial fordisrupting pathogen membranes.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001120921400001},
      doi          = {10.1002/pro.4818},
      url          = {https://juser.fz-juelich.de/record/1021663},
}