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@ARTICLE{Larsen:861865,
      author       = {Larsen, Andreas Haahr and Dorosz, Jerzy and Thorsen, Thor
                      Seneca and Johansen, Nicolai Tidemand and Darwish, Tamim and
                      Midtgaard, Søren Roi and Arleth, Lise and Kastrup, Jette
                      Sandholm},
      title        = {{S}mall-angle neutron scattering studies on the {AMPA}
                      receptor {G}lu{A}2 in the resting, {AMPA}-bound and
                      {GYKI}-53655-bound states},
      journal      = {IUCrJ},
      volume       = {5},
      number       = {6},
      issn         = {2052-2525},
      address      = {Chester},
      reportid     = {FZJ-2019-02286},
      pages        = {780 - 793},
      year         = {2018},
      abstract     = {The AMPA receptor GluA2 belongs to the family of ionotropic
                      glutamate receptors, which are responsible for most of the
                      fast excitatory neuronal signalling in the central nervous
                      system. These receptors are important for memory and
                      learning, but have also been associated with brain diseases
                      such as Alzheimer's disease and epilepsy. Today, one drug is
                      on the market for the treatment of epilepsy targeting AMPA
                      receptors, i.e. a negative allosteric modulator of these
                      receptors. Recently, crystal structures and cryo-electron
                      microscopy (cryo-EM) structures of full-length GluA2 in the
                      resting (apo), activated and desensitized states have been
                      reported. Here, solution structures of full-length GluA2 are
                      reported using small-angle neutron scattering (SANS) with a
                      novel, fully matched-out detergent. The GluA2 solution
                      structure was investigated in the resting state as well as
                      in the presence of AMPA and of the negative allosteric
                      modulator GYKI-53655. In solution and at neutral pH, the
                      SANS data clearly indicate that GluA2 is in a compact form
                      in the resting state. The solution structure resembles the
                      crystal structure of GluA2 in the resting state, with an
                      estimated maximum distance (Dmax) of 179 ± 11 Å and a
                      radius of gyration (Rg) of 61.9 ± 0.4 Å. An ab initio
                      model of GluA2 in solution generated using DAMMIF clearly
                      showed the individual domains, i.e. the extracellular
                      N-terminal domains and ligand-binding domains as well as the
                      transmembrane domain. Solution structures revealed that
                      GluA2 remained in a compact form in the presence of AMPA or
                      GYKI-53655. At acidic pH only, GluA2 in the presence of AMPA
                      adopted a more open conformation of the extracellular part
                      (estimated Dmax of 189 ± 5 Å and Rg of 65.2 ±
                      0.5 Å), resembling the most open, desensitized class 3
                      cryo-EM structure of GluA2 in the presence of quisqualate.
                      In conclusion, this methodological study may serve as an
                      example for future SANS studies on membrane proteins.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30443361},
      UT           = {WOS:000448982300014},
      doi          = {10.1107/S2052252518012186},
      url          = {https://juser.fz-juelich.de/record/861865},
}