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@ARTICLE{Sluchanko:398520,
      author       = {Sluchanko, Nikolai N. and Tugaeva, Kristina V. and
                      Maksimov, Eugene G.},
      title        = {{S}olution structure of human steroidogenic acute
                      regulatory protein {STARD}1 studied by small-angle {X}-ray
                      scattering},
      journal      = {Biochemical and biophysical research communications},
      volume       = {489},
      number       = {4},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PUBDB-2017-14090},
      pages        = {445 - 450},
      year         = {2017},
      abstract     = {Intracellular cholesterol transfer to mitochondria, a
                      bottleneck of adrenal and gonadal steroidogenesis, relies on
                      the functioning of the steroidogenic acute regulatory
                      protein (StAR, STARD1), for which many disease-associated
                      mutations have been described. Despite significant progress
                      in the field, the exact mechanism of cholesterol binding and
                      transfer by STARD1 still remains debatable and often
                      considers significant structural rearrangements to achieve
                      ligand binding. The crystal structure of STARD1, obtained
                      recently at medium resolution, suggests that this protein
                      has the same fold as other members of the START family.
                      However, hydrodynamic properties and solution conformation
                      of STARD1 are insufficiently characterized, partially due to
                      poor solubility of this protein. Here, we used our recent
                      protocol to obtain stable and soluble STARD1 and analyzed
                      its hydrodynamic properties and solution conformation using
                      a previously inapplicable small-angle X-ray scattering
                      (SAXS). The SAXS data obtained exclusively from a
                      monodisperse fraction of the monomeric protein suggest that,
                      apart from movements of the flexible Ω1-loop, STARD1
                      unlikely undergoes significant spontaneous rearrangements
                      proposed earlier as a gating mechanism for cholesterol
                      binding. The consistency with the previously reported
                      solution NMR structure of STARD6 suggests similarity of
                      hydrodynamic behavior of other STARD-containing proteins.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28576490},
      UT           = {WOS:000404203000014},
      doi          = {10.1016/j.bbrc.2017.05.167},
      url          = {https://bib-pubdb1.desy.de/record/398520},
}