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@ARTICLE{Kozlowska:206135,
      author       = {Kozlowska , Malgorzata and Tarczewska, Aneta and michał,
                      jakób and Szpotkowski, Kamil and Wojtas, Magdalena and
                      Andrzej, Ozyhar},
      title        = {{C}alponin-{L}ike {C}hd64 {I}s {P}artly {D}isordered},
      journal      = {PLoS one},
      volume       = {9},
      number       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2015-00661},
      pages        = {e96809},
      year         = {2014},
      note         = {OA},
      abstract     = {20-hydroxyecdysone (20E) and juvenile hormone (JH)
                      signaling pathways interact to regulate insect development.
                      Recently,two proteins, a calponin-like Chd64 and
                      immunophilin FKBP39 have been found to play a pivotal role
                      in the cross-talkbetween 20E and JH, although the molecular
                      basis of interaction remains unknown. The aim of this work
                      was to identify thestructural features that would provide
                      understanding of the role of Chd64 in multiple and dynamic
                      complex that cross-linksthe signaling pathways. Here, we
                      demonstrate the results of in silico and in vitro analyses
                      of the structural organization ofChd64 from Drosophila
                      melanogaster and its homologue from Tribolium castaneum.
                      Computational analysis predicted theexistence of disordered
                      regions on the termini of both proteins, while the central
                      region appeared to be globular, probablycorresponding to the
                      calponin homology (CH) domain. In vitro analyses of the
                      hydrodynamic properties of the proteinsfrom analytical
                      size-exclusion chromatography and analytical
                      ultracentrifugation revealed that DmChd64 and TcChd64 hadan
                      asymmetrical, elongated shape, which was further confirmed
                      by small angle X-ray scattering (SAXS). The Kratky
                      plotindicated disorderness in both Chd64 proteins, which
                      could possibly be on the protein termini and which would
                      give rise tospecific hydrodynamic properties. Disordered
                      tails are often involved in diverse interactions. Therefore,
                      it is highly possiblethat there are intrinsically disordered
                      regions (IDRs) on both termini of the Chd64 proteins that
                      serve as platforms formultiple interaction with various
                      partners and constitute the foundation for their regulatory
                      function.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {PETRA Beamline P13 (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-P13-20130405},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000335728900099},
      pubmed       = {pmid:24805353},
      doi          = {10.1371/journal.pone.0096809},
      url          = {https://bib-pubdb1.desy.de/record/206135},
}