Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates α-helix formation of the polyQ tract but suppresses its aggregation

• Published in: Scientific reports Vol. 9; no. 1; p. 7481
• Main Authors: Hong, Jun-Ye, Wang, Dong-Dong, Xue, Wei, Yue, Hong-Wei, Yang, Hui, Jiang, Lei-Lei, Wang, Wen-Ning, Hu, Hong-Yu
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 16.05.2019; Nature Publishing Group
• Subjects: 140/131; 631/45/470/2284; 631/57/2272; 82; Alanine; Amyloid; Amyloid - chemistry; Amyloid - metabolism; Ataxia; Ataxin; Ataxin-7 - chemistry; Ataxin-7 - metabolism; Disease; HEK293 Cells; Humanities and Social Sciences; Humans; Laboratories; Molecular Dynamics Simulation; multidisciplinary; N-Terminus; Pathogenesis; Peptides - chemistry; Polyglutamine; Population; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Multimerization; Proteins; Science; Science (multidisciplinary); Spinocerebellar ataxia; Trinucleotide repeat diseases

Ataxin-7 (Atx7) is a disease-related protein associated with the pathogenesis of spinocerebellar ataxia 7, while its polyglutamine (polyQ) tract in N-terminus is the causative source of aggregation and proteinopathy. We investigated the structure, dynamics and aggregation properties of the N-termina...