Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of va...
Enregistré dans:
| Auteurs principaux: | , , , , , , , , , , , |
|---|---|
| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2021
|
| Sujets: | |
| Accès en ligne: | https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
| Résumé: | Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of various HTTex1 fibril types with different toxicity and find that the dynamics and entanglement of the PRD domain differs among them and that the HTTex1 fibrils can be interconverted. |
|---|