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@ARTICLE{Dioletis:139937,
      author       = {Dioletis, Evangelos and Dingley, Andrew and Driscoll, Paul
                      C},
      title        = {{S}tructural and functional characterization of the
                      recombinant death domain from death-associated protein
                      kinase.},
      journal      = {PLoS one},
      volume       = {8},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2013-05904},
      pages        = {e70095},
      year         = {2013},
      abstract     = {Death-associated protein kinase (DAPk) is a
                      calcium/calmodulin-regulated Ser/Thr-protein kinase that
                      functions at an important point of integration for cell
                      death signaling pathways. DAPk has a structurally unique
                      multi-domain architecture, including a C-terminally
                      positioned death domain (DD) that is a positive regulator of
                      DAPk activity. In this study, recombinant DAPk-DD was
                      observed to aggregate readily and could not be prepared in
                      sufficient yield for structural analysis. However, DAPk-DD
                      could be obtained as a soluble protein in the form of a
                      translational fusion protein with the B1 domain of
                      streptococcal protein G. In contrast to other DDs that adopt
                      the canonical six amphipathic α-helices arranged in a
                      compact fold, the DAPk-DD was found to possess surprisingly
                      low regular secondary structure content and an absence of a
                      stable globular fold, as determined by circular dichroism
                      (CD), NMR spectroscopy and a temperature-dependent
                      fluorescence assay. Furthermore, we measured the in vitro
                      interaction between extracellular-regulated kinase-2 (ERK2)
                      and various recombinant DAPk-DD constructs. Despite the low
                      level of structural order, the recombinant DAPk-DD retained
                      the ability to interact with ERK2 in a 1∶1 ratio with a K
                      d in the low micromolar range. Only the full-length DAPk-DD
                      could bind ERK2, indicating that the apparent 'D-motif'
                      located in the putative sixth helix of DAPk-DD is not
                      sufficient for ERK2 recognition. CD analysis revealed that
                      binding of DAPk-DD to ERK2 is not accompanied by a
                      significant change in secondary structure. Taken together
                      our data argue that the DAPk-DD, when expressed in
                      isolation, does not adopt a classical DD fold, yet in this
                      state retains the capacity to interact with at least one of
                      its binding partners. The lack of a stable globular
                      structure for the DAPk-DD may reflect either that its
                      folding would be supported by interactions absent in our
                      experimental set-up, or a limitation in the structural
                      bioinformatics assignment of the three-dimensional
                      structure.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23922916},
      pmc          = {pmc:PMC3726526},
      UT           = {WOS:000323369700132},
      doi          = {10.1371/journal.pone.0070095},
      url          = {https://juser.fz-juelich.de/record/139937},
}