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@ARTICLE{Oroz:140876,
      author       = {Oroz, Javier and Blair, Laura J and Zweckstetter, Markus},
      title        = {{D}ynamic {A}ha1 co-chaperone binding to human {H}sp90.},
      journal      = {Protein science},
      volume       = {28},
      number       = {9},
      issn         = {0961-8368},
      address      = {Bethesda, Md.},
      publisher    = {Protein Society},
      reportid     = {DZNE-2020-07198},
      pages        = {1545-1551},
      year         = {2019},
      abstract     = {Hsp90 is an essential chaperone that requires large
                      allosteric changes to determine its ATPase activity and
                      client binding. The co-chaperone Aha1, which is the major
                      ATPase stimulator in eukaryotes, is important for regulation
                      of Hsp90's allosteric timing. Little is known, however,
                      about the structure of the Hsp90/Aha1 complex. Here, we
                      characterize the solution structure of unmodified human
                      Hsp90/Aha1 complex using NMR spectroscopy. We show that the
                      214-kDa complex forms by a two-step binding mechanism and
                      adopts multiple conformations in the absence of nucleotide.
                      Aha1 induces structural changes near Hsp90's
                      nucleotide-binding site, providing a basis for its
                      ATPase-enhancing activity. Our data reveal important aspects
                      of this pivotal chaperone/co-chaperone interaction and
                      emphasize the relevance of characterizing dynamic chaperone
                      structures in solution.},
      keywords     = {Allosteric Regulation / Binding Sites / HSP90 Heat-Shock
                      Proteins: chemistry / HSP90 Heat-Shock Proteins: metabolism
                      / Humans / Models, Molecular / Molecular Chaperones:
                      chemistry / Molecular Chaperones: metabolism / Molecular
                      Weight / Nuclear Magnetic Resonance, Biomolecular / Protein
                      Binding / Protein Conformation},
      cin          = {AG Zweckstetter},
      ddc          = {610},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31299134},
      pmc          = {pmc:PMC6699087},
      doi          = {10.1002/pro.3678},
      url          = {https://pub.dzne.de/record/140876},
}