% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Ponzoni:827445,
      author       = {Ponzoni, Luca and Rossetti, Giulia and Maggi, Luca and
                      Giorgetti, Alejandro and Carloni, Paolo and Micheletti,
                      Cristian},
      title        = {{U}nifying view of mechanical and functional hotspots
                      across class {A} {GPCR}s},
      journal      = {PLoS Computational Biology},
      volume       = {13},
      number       = {2},
      issn         = {1553-7358},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {FZJ-2017-01570},
      pages        = {e1005381 -},
      year         = {2017},
      abstract     = {G protein-coupled receptors (GPCRs) are the largest
                      superfamily of signaling proteins. Their activation process
                      is accompanied by conformational changes that have not yet
                      been fully uncovered. Here, we carry out a novel comparative
                      analysis of internal structural fluctuations across a
                      variety of receptors from class A GPCRs, which currently has
                      the richest structural coverage. We infer the local
                      mechanical couplings underpinning the receptors’
                      functional dynamics and finally identify those amino acids
                      whose virtual deletion causes a significant softening of the
                      mechanical network. The relevance of these amino acids is
                      demonstrated by their overlap with those known to be crucial
                      for GPCR function, based on static structural criteria. The
                      differences with the latter set allow us to identify those
                      sites whose functional role is more clearly detected by
                      considering dynamical and mechanical properties. Of these
                      sites with a genuine mechanical/dynamical character, the top
                      ranking is amino acid 7x52, a previously unexplored, and
                      experimentally verifiable key site for GPCR conformational
                      response to ligand binding.},
      cin          = {IAS-5 / INM-11 / INM-9 / JSC / JARA-HPC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-11-20170113 /
                      I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)JSC-20090406 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511) /
                      Towards the design of allosteric ligands binding to the
                      human muscarinic receptor M2 $(jias59_20161101)$},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511 /
                      $G:(DE-Juel1)jias59_20161101$},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000395718800027},
      pubmed       = {pmid:28158180},
      doi          = {10.1371/journal.pcbi.1005381},
      url          = {https://juser.fz-juelich.de/record/827445},
}