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@ARTICLE{Shimanovskaya:207425,
      author       = {Shimanovskaya, Ekaterina and Viscardi, Valeria and
                      Lesigang, Johannes and Lettman, Molly M. and Qiao, Renping
                      and Svergun, Dmitri and Round, Adam and Oegema, Karen and
                      Dong, Gang},
      title        = {{S}tructure of the {C}. {E}legans {ZYG}-1 {C}ryptic {P}olo
                      {B}ox {S}uggests a {C}onserved {M}echanism for {C}entriolar
                      {D}ocking of {P}lk4 {K}inases},
      journal      = {Structure},
      volume       = {22},
      number       = {8},
      issn         = {0969-2126},
      address      = {London [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PUBDB-2015-01335},
      pages        = {1090 - 1104},
      year         = {2014},
      note         = {(c) Elsevier Ltd. Post referee full text in progress.},
      abstract     = {Plk4 family kinases control centriole assembly. Plk4s
                      target mother centrioles through an interaction between
                      their cryptic polo box (CPB) and acidic regions in the
                      centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152.
                      Here, we report a crystal structure for the CPB of C.
                      elegans ZYG-1, which forms a Z-shaped dimer containing an
                      intermolecular β sheet with an extended basic surface
                      patch. Biochemical and in vivo analysis revealed that
                      electrostatic interactions dock the ZYG-1 CPB basic patch
                      onto the SPD-2-derived acidic region to promote ZYG-1
                      targeting and new centriole assembly. Analysis of a
                      different crystal form of the Drosophila Plk4 (DmPlk4) CPB
                      suggests that it also forms a Z-shaped dimer. Comparison of
                      the ZYG-1 and DmPlk4 CPBs revealed structural changes in the
                      ZYG-1 CPB that confer selectivity for binding SPD-2 over
                      Asterless-derived acidic regions. Overall, our findings
                      suggest a conserved mechanism for centriolar docking of Plk4
                      homologs that initiate daughter centriole assembly.},
      cin          = {EMBL / DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)HAS-User-20120731},
      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},
      UT           = {WOS:000340488100004},
      pubmed       = {pmid:24980795},
      doi          = {10.1016/j.str.2014.05.009},
      url          = {https://bib-pubdb1.desy.de/record/207425},
}