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@ARTICLE{Fodor:293439,
      author       = {Fodor, Krisztián and Wolf, Janina and Reglinski, Katharina
                      and Passon, Daniel M. and Lou, Ye and Schliebs, Wolfgang and
                      Erdmann, Ralf and Wilmanns, Matthias},
      title        = {{L}igand-{I}nduced {C}ompaction of the {PEX}5
                      {R}eceptor-{B}inding {C}avity {I}mpacts {P}rotein {I}mport
                      {E}fficiency into {P}eroxisomes},
      journal      = {Traffic},
      volume       = {16},
      number       = {1},
      issn         = {1398-9219},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {PUBDB-2016-00528},
      pages        = {85 - 98},
      year         = {2015},
      note         = {(c) John Wiley $\&$ Sons A/S. Published by John Wiley $\&$
                      Sons Ltd. Post referee full text in progress.},
      abstract     = {Peroxisomes entirely rely on the import of their proteome
                      across the peroxisomal membrane. Recognition efficiencies of
                      peroxisomal proteins vary by more than 1000-fold, but the
                      molecular rationale behind their subsequent differential
                      import and sorting has remained enigmatic. Using the protein
                      cargo alanine-glyoxylate aminotransferase as a model, an
                      unexpected increase from 34 to $80\%$ in peroxisomal import
                      efficiency of a single-residue mutant has been discovered.
                      By high-resolution structural analysis, we found that it is
                      the recognition receptor PEX5 that adapts its conformation
                      for high-affinity binding rather than the cargo protein
                      signal motif as previously thought. During receptor
                      recognition, the binding cavity of the receptor shrinks to
                      one third of its original volume. This process is impeded in
                      the wild-type protein cargo because of a bulky side chain
                      within the recognition motif, which blocks contraction of
                      the PEX5 binding cavity. Our data provide a new insight into
                      direct protein import efficiency by removal rather than by
                      addition of an apparent specific sequence signature that is
                      generally applicable to peroxisomal matrix proteins and to
                      other receptor recognition processes.},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000346733300006},
      pubmed       = {pmid:25369882},
      doi          = {10.1111/tra.12238},
      url          = {https://bib-pubdb1.desy.de/record/293439},
}