Structural features and domain organization of huntingtin fibrils.

  title={Structural features and domain organization of huntingtin fibrils.},
  author={Charles W. Bugg and Jose Mario Isas and Torsten Fischer and Paul H. Patterson and Ralf Langen},
  journal={The Journal of biological chemistry},
  volume={287 38},
Misfolding and aggregation of huntingtin is one of the hallmarks of Huntington disease, but the overall structure of these aggregates and the mechanisms by which huntingtin misfolds remain poorly understood. Here we used site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy to study the structural features of huntingtin exon 1 (HDx1) containing 46 glutamine residues in its polyglutamine (polyQ) region. Despite some residual structuring in the N terminus, we find… CONTINUE READING