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@ARTICLE{Gao:18855,
      author       = {Gao, S and von der Malsburg, A. and Dick, A. and Faelber,
                      K. and Schröder, G.F. and Haller, O. and Kochs, G. and
                      Daumke, O.},
      title        = {{S}tructure of {M}yxovirus {R}esistance {P}rotein {A}
                      {R}eveals {I}ntra- and {I}ntermolecular {D}omain
                      {I}nteractions {R}equired for the {A}ntiviral {F}unction},
      journal      = {Immunity},
      volume       = {35},
      issn         = {1074-7613},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {PreJuSER-18855},
      pages        = {514 - 525},
      year         = {2011},
      note         = {This project was supported by grants of the Deutsche
                      Forschungsgemeinschaft (SFB 740/TP C7 and SFB958/A12 to O.D.
                      and Ko1579/8-1 to G.K.), by a Career Development Fellowship
                      of The International Human Frontier Science Program
                      Organization, and by the EMBO Young Investigator Program to
                      O.D. We are grateful to A. Brunger for providing us with the
                      prerelease of CNS version 1.3, the BESSY staff at beamline
                      BL14.1 and SLS staff at beamline X06SA for help with data
                      collection, and S. Werner, S. Paeschke, and S. Gruber for
                      technical assistance.},
      abstract     = {Human myxovirus resistance protein 1 (MxA) is an
                      interferon-induced dynamin-like GTPase that acts as a
                      cell-autonomous host restriction factor against many viral
                      pathogens including influenza viruses. To study the
                      molecular principles of its antiviral activity, we
                      determined the crystal structure of nucleotide-free MxA,
                      which showed an extended three-domain architecture. The
                      central bundle signaling element (BSE) connected the
                      amino-terminal GTPase domain with the stalk via two hinge
                      regions. MxA oligomerized in the crystal via the stalk and
                      the BSE, which in turn interacted with the stalk of
                      the neighboring monomer. We demonstrated that the intra-
                      and intermolecular domain interplay between the BSE and
                      stalk was essential for oligomerization and the antiviral
                      function of MxA. Based on these results, we propose a
                      structural model for the mechano-chemical coupling in
                      ring-like MxA oligomers as the principle mechanism for this
                      unique antiviral effector protein.},
      keywords     = {Animals / Cell Line / Crystallography, X-Ray / GTP-Binding
                      Proteins: chemistry / Humans / Models, Molecular / Protein
                      Structure, Quaternary / Protein Structure, Tertiary /
                      Structural Homology, Protein / myxovirus resistance proteins
                      (NLM Chemicals) / GTP-Binding Proteins (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Immunology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21962493},
      UT           = {WOS:000296657700011},
      doi          = {10.1016/j.immuni.2011.07.012},
      url          = {https://juser.fz-juelich.de/record/18855},
}