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@ARTICLE{Kaushik:638199,
      author       = {Kaushik, Vineeta and Gessa, Luca and Kumar, Nelam and
                      Pinkas, Matyáš and Czarnocki-Cieciura, Mariusz and
                      Palczewski, Krzysztof and Nováček, Jiří and Fernandes,
                      Humberto},
      title        = {{C}ryo{EM} structure and small-angle {X}-ray scattering
                      analyses of porcine retinol-binding protein 3},
      journal      = {Open biology},
      volume       = {15},
      number       = {1},
      issn         = {2046-2441},
      address      = {London},
      publisher    = {Royal Society Publishing},
      reportid     = {PUBDB-2025-04017},
      pages        = {240180},
      year         = {2025},
      abstract     = {The vertebrate visual cycle hinges on enzymatically
                      converting all-trans-retinol (at-ROL) into 11-cis-retinal
                      (11c-RAL), the chromophore that binds to opsins in
                      photoreceptors, forming light-responsive pigments. When
                      struck by a photon, these pigments activate the
                      phototransduction pathway and initiate the process of
                      vision. The enzymatic isomerization of at-ROL, crucial for
                      restoring the visual pigments and preparing them to receive
                      new light stimuli, relies on various enzymes found in both
                      the photoreceptors and retinal pigment epithelium cells. To
                      function effectively, retinoids must shuttle between these
                      two cell types. Retinol-binding protein 3 (RBP3), located in
                      the interphotoreceptor matrix, probably plays a pivotal role
                      in this transport mechanism. Comprised of four
                      retinoid-binding modules, RBP3 also binds fatty acids,
                      potentially aiding retinal function by facilitating the
                      loading and unloading of different retinoids at specific
                      cell types thereby directing the cycle. In this study, we
                      present a 3.67 Å cryoEM structure of porcine RBP3, along
                      with molecular docking analysis and corroborative
                      in-solution small-angle X-ray scattering data for titration
                      of RBP3 with relevant ligands, that also give insights on
                      RBP3 conformational adaptability.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1098/rsob.240180},
      url          = {https://bib-pubdb1.desy.de/record/638199},
}