Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted

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...

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Bibliographic Details
Main Authors: J. Mario Isas, Nitin K. Pandey, Hui Xu, Kazuki Teranishi, Alan K. Okada, Ellisa K. Fultz, Anoop Rawat, Anise Applebaum, Franziska Meier, Jeannie Chen, Ralf Langen, Ansgar B. Siemer
Format: article
Language:EN
Published: Nature Portfolio 2021
Subjects:
Science
Q
Online Access:https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a
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Summary: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.

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