Faculty, Staff and Student Publications
Language
English
Publication Date
4-1-2026
Journal
Journal of Biomolecular Structure and Dynamics
DOI
10.1080/07391102.2025.2474683
PMID
40091796
PMCID
PMC12353482
Abstract
Huntington's disease (HD) is a neurodegenerative disorder caused by an abnormal CAG expansion in the Huntingtin (HTT) gene. Given its simple genetic cause but complex pathogenic mechanisms, interest in targeting HTT for HD treatment is growing, necessitating a clear understanding of HTT regulation. HTT protein primarily exists in a core complex with HAP40, forming a highly ordered structure with two large globular domains connected by a bridge. We previously demonstrated that HAP40 is conserved in
Keywords
Animals, Humans, Huntingtin Protein, Drosophila Proteins, Protein Binding, Huntington Disease, Molecular Dynamics Simulation, Models, Molecular, Drosophila, Structure-Activity Relationship, Drosophila melanogaster, Amino Acid Sequence
Published Open-Access
yes
Recommended Citation
Farmer, Stephen M; Solbach, Amanda; Xu, Shiyu; et al., "Structural-Functional Analyses of the Huntingtin/HAP40 Complex in Drosophila and Humans" (2026). Faculty, Staff and Student Publications. 6835.
https://digitalcommons.library.tmc.edu/uthgsbs_docs/6835
Included in
Bioinformatics Commons, Biomedical Informatics Commons, Genetic Phenomena Commons, Medical Genetics Commons, Oncology Commons