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Article

The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain.

Structure (London, England : 1993) - 1 Sept 2020

Jung Taeyang, Shin Baehyun, Tamo Giorgio, Kim Hyeongju, Vijayvargia Ravi, Leitner Alexander, Marcaida Maria J, Astorga-Wells Juan, Jung Roy, Aebersold Ruedi, Peraro Matteo Dal, Hebert Hans, Seong Ihn Sik, Song Ji-Joon

Abstract excerpt

The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural information on its HEAT-repeat domains. Here, we present analyses of the impact of polyQ length on the structure and function of HTT via an integrative structural and biochemical approach. The cryo-EM analysis of normal...

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Identifiers

PMID: 32668197
DOI: 10.1016/j.str.2020.06.008
PMCID: PMC11059206

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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