Implications of the Orb2 Amyloid Structure in Huntington's Disease

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2020 Sep 24

PMID 32967102

Authors

Ruben Hervas

Alexey G Murzin

Kausik Si

Affiliations

Soon will be listed here.

Abstract

Huntington's disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington's disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from brain and how this information provides plausible structural insight on the structure of huntingtin deposits in the brain.

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