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@ARTICLE{Motz:141093,
      author       = {Motz, C. and Schuhmann, K. M. and Kirchhofer, A. and Moldt,
                      M. and Witte, G. and Conzelmann, K.-K. and Hopfner, K.-P.
                      and DESY},
      title        = {{P}aramyxovirus {V} {P}roteins {D}isrupt the {F}old of the
                      {RNA} {S}ensor {MDA}5 to {I}nhibit {A}ntiviral {S}ignaling},
      journal      = {Science},
      volume       = {339},
      issn         = {0036-8075},
      reportid     = {PHPPUBDB-24959},
      pages        = {693},
      year         = {2013},
      note         = {Post referee fulltext in progress; Embargo 6 months from
                      publication},
      abstract     = {The retinoic acid-inducible gene I (RIG-I)-like receptor
                      (RLR) melanoma differentiation-associated protein 5 (MDA5)
                      senses cytoplasmic viral RNA and activates antiviral innate
                      immunity. To reveal how paramyxoviruses counteract this
                      response, we determined the crystal structure of the MDA5
                      adenosine 5'-triphosphate (ATP)-hydrolysis domain in complex
                      with the viral inhibitor V protein. The V protein unfolded
                      the ATP-hydrolysis domain of MDA5 via a β-hairpin motif and
                      recognized a structural motif of MDA5 that is normally
                      buried in the conserved helicase fold. This leads to
                      disruption of the MDA5 ATP-hydrolysis site and prevention of
                      RNA-bound MDA5 filament formation. The structure explains
                      why V proteins inactivate MDA5, but not RIG-I, and mutating
                      only two amino acids in RIG-I induces robust V protein
                      binding. Our results suggest an inhibition mechanism of RLR
                      signalosome formation by unfolding of receptor and
                      inhibitor.},
      keywords     = {Adenosine Triphosphate: metabolism / Amino Acid Motifs /
                      Amino Acid Sequence / Animals / Crystallography, X-Ray /
                      DEAD-box RNA Helicases: chemistry / DEAD-box RNA Helicases:
                      genetics / DEAD-box RNA Helicases: metabolism / HEK293 Cells
                      / Humans / Hydrolysis / Immunity, Innate / Mice / Models,
                      Molecular / Molecular Sequence Data / Mutation / Protein
                      Binding / Protein Folding / Protein Structure, Tertiary /
                      RNA, Double-Stranded: metabolism / Signal Transduction /
                      Simian virus 5: immunology / Sus scrofa / Viral Proteins:
                      chemistry / Viral Proteins: genetics / Viral Proteins:
                      metabolism / RNA, Double-Stranded (NLM Chemicals) / V
                      protein, Paramyxovirus (NLM Chemicals) / Viral Proteins (NLM
                      Chemicals) / Adenosine Triphosphate (NLM Chemicals) / DDX58
                      protein, human (NLM Chemicals) / DEAD-box RNA Helicases (NLM
                      Chemicals) / IFIH1 protein, human (NLM Chemicals)},
      cin          = {HASYLAB(-2012) / EMBL(-2012)},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23328395},
      UT           = {WOS:000314585600041},
      doi          = {10.1126/science.1230949},
      url          = {https://bib-pubdb1.desy.de/record/141093},
}