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@ARTICLE{GmezVelasco:638197,
      author       = {Gómez-Velasco, Homero and García-Ramírez, Benjamín and
                      Siliqi, Dritan and Graewert, Melissa A. and
                      Quintero-Martinez, Adrián and Ortega, Enrique and
                      Rodríguez-Romero, Adela},
      title        = {{A}llergen-induced structural rearrangements in {I}g{E}:
                      insights from {SAXS} and molecular dynamics},
      journal      = {International journal of biological macromolecules},
      volume       = {328},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2025-04015},
      pages        = {147658 -},
      year         = {2025},
      abstract     = {The initiation of allergic responses critically depends on
                      the recognition of an allergenic epitope by the paratope of
                      IgE antibodies. While previous structural studies have
                      focused on recombinant fragments or engineered forms of IgE,
                      the structure of full-length IgE in its native state remains
                      poorly understood. In this study, we investigate the
                      conformational changes of a native murine IgE (2F5), both in
                      its free form and upon binding to the Hevea brasiliensis
                      allergen profilin (Hev b 8). Small-angle X-ray scattering
                      (SAXS) data reveal that unbound IgE adopts an extended
                      conformation with open Fab arms. However, when it binds to
                      profilin, it transitions to a more compact arrangement
                      characterized by closer proximity of the arms. Molecular
                      dynamics (MD) simulations of the Fab region further
                      identified conformational rearrangements upon allergen
                      binding, including a twisting motion and partial disruption
                      of interactions between the naturally paired heavy and light
                      chains. These findings indicate that there may be allosteric
                      communication between Fab and Fc regions, even in the
                      absence of a hinge region, which is not present in IgE.
                      Overall, this study provides valuable insights into the
                      dynamic structural properties of native IgE and enhances our
                      understanding of the molecular mechanisms underlying
                      allergen recognition.},
      cin          = {EMBL-User / EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.ijbiomac.2025.147658},
      url          = {https://bib-pubdb1.desy.de/record/638197},
}