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@ARTICLE{Maggi:873035,
      author       = {Maggi, L. and Carloni, P. and Rossetti, G.},
      title        = {{M}odeling the allosteric modulation on a {G}-{P}rotein
                      {C}oupled {R}eceptor: the case of {M}2 muscarinic
                      {A}cetylcholine {R}eceptor in complex with {LY}211960},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-00486},
      pages        = {3037},
      year         = {2020},
      abstract     = {Allosteric modulation is involved in a plethora of diverse
                      protein functions, which are fundamental for cells’ life.
                      This phenomenon can be thought as communication between two
                      topographically distinct site of a protein structure. How
                      this communication occurs is still matter of debate. Many
                      different descriptions have been presented so far. Here we
                      consider a specific case where any significant
                      conformational change is involved upon allosteric modulator
                      binding and the phenomenon is depicted as a vibrational
                      energy diffusion process between distant protein regions. We
                      applied this model, by employing computational tools, to the
                      human muscarinic receptor M2, a transmembrane protein
                      G-protein coupled receptor known to undergo allosteric
                      modulation whose recently X-ray structure has been recently
                      resolved both with and without the presence of a particular
                      allosteric modulator. Our calculations, performed on these
                      two receptor structures, suggest that for this case the
                      allosteric modulator modifies the energy current between
                      functionally relevant regions of the protein; this allows to
                      identify the main residues responsible for this modulation.
                      These results contribute to shed light on the molecular
                      basis of allosteric modulation and may help design new
                      allosteric ligands.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32080232},
      UT           = {WOS:000563079900021},
      doi          = {10.1038/s41598-020-59289-5},
      url          = {https://juser.fz-juelich.de/record/873035},
}