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@ARTICLE{UkmarGodec:270413,
      author       = {Ukmar-Godec, Tina and Yu, Taekyung and Ibanez de Opakua,
                      Alain and Pantoja, Christian F and Munari, Francesca and
                      Zweckstetter, Markus},
      title        = {{C}onformational diversity of human {HP}1α.},
      journal      = {Protein science},
      volume       = {33},
      number       = {7},
      issn         = {0961-8368},
      address      = {Bethesda, Md.},
      publisher    = {Protein Society},
      reportid     = {DZNE-2024-00793},
      pages        = {e5079},
      year         = {2024},
      abstract     = {Heterochromatin protein 1 alpha (HP1α) is an
                      evolutionarily conserved protein that binds chromatin and is
                      important for gene silencing. The protein comprises 191
                      residues arranged into three disordered regions and two
                      structured domains, the chromo and chromoshadow domain,
                      which associates into a homodimer. While high-resolution
                      structures of the isolated domains of HP1 proteins are
                      known, the structural properties of full-length HP1α remain
                      largely unknown. Using a combination of NMR spectroscopy and
                      structure predictions by AlphaFold2 we provide evidence that
                      the chromo and chromoshadow domain of HP1α engage in direct
                      contacts resulting in a compact chromo/chromoshadow domain
                      arrangement. We further show that HP1β and HP1γ have
                      increased interdomain dynamics when compared to HP1α which
                      may contribute to the distinct roles of different Hp1
                      isoforms in gene silencing and activation.},
      keywords     = {Chromobox Protein Homolog 5: chemistry / Chromosomal
                      Proteins, Non-Histone: chemistry / Chromosomal Proteins,
                      Non-Histone: genetics / Chromosomal Proteins, Non-Histone:
                      metabolism / Humans / Models, Molecular / Nuclear Magnetic
                      Resonance, Biomolecular / Protein Domains / Protein
                      Conformation / HP1α (Other) / AlphaFold (Other) / HP1α
                      (Other) / NMR spectroscopy (Other) / chromatin (Other) /
                      dynamics (Other) / residual dipolar couplings (Other) /
                      Chromobox Protein Homolog 5 (NLM Chemicals) / Chromosomal
                      Proteins, Non-Histone (NLM Chemicals) / CBX5 protein, human
                      (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {610},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38895997},
      pmc          = {pmc:PMC11187854},
      doi          = {10.1002/pro.5079},
      url          = {https://pub.dzne.de/record/270413},
}