Structural disorder of monomeric α-synuclein persists in mammalian cells

  title={Structural disorder of monomeric α-synuclein persists in mammalian cells},
  author={François-Xavier Theillet and Andr{\'e}s Binolfi and Beata Bekei and Andrea Martorana and Honor May Rose and Marchel Stuiver and Silvia Verzini and Dorothea Lorenz and Marleen van Rossum and Daniella Goldfarb and Philipp Selenko},
Intracellular aggregation of the human amyloid protein α-synuclein is causally linked to Parkinson’s disease. While the isolated protein is intrinsically disordered, its native structure in mammalian cells is not known. Here we use nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to derive atomic-resolution insights into the structure and dynamics of α-synuclein in different mammalian cell types. We show that the disordered nature of monomeric α-synuclein… CONTINUE READING
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Parkinson-causing alpha-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

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