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TitleHuntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 1374, Year 2021
Publish dateDec 8, 2021
AuthorsRachel J Harding / Justin C Deme / Johannes F Hevler / Sem Tamara / Alexander Lemak / Jeffrey P Cantle / Magdalena M Szewczyk / Nola Begeja / Siobhan Goss / Xiaobing Zuo / Peter Loppnau / Alma Seitova / Ashley Hutchinson / Lixin Fan / Ray Truant / Matthieu Schapira / Jeffrey B Carroll / Albert J R Heck / Susan M Lea / Cheryl H Arrowsmith /
PubMed AbstractHuntington's disease results from expansion of a glutamine-coding CAG tract in the huntingtin (HTT) gene, producing an aberrantly functioning form of HTT. Both wildtype and disease-state HTT form a ...Huntington's disease results from expansion of a glutamine-coding CAG tract in the huntingtin (HTT) gene, producing an aberrantly functioning form of HTT. Both wildtype and disease-state HTT form a hetero-dimer with HAP40 of unknown functional relevance. We demonstrate in vivo and in cell models that HTT and HAP40 cellular abundance are coupled. Integrating data from a 2.6 Å cryo-electron microscopy structure, cross-linking mass spectrometry, small-angle X-ray scattering, and modeling, we provide a near-atomic-level view of HTT, its molecular interaction surfaces and compacted domain architecture, orchestrated by HAP40. Native mass spectrometry reveals a remarkably stable hetero-dimer, potentially explaining the cellular inter-dependence of HTT and HAP40. The exon 1 region of HTT is dynamic but shows greater conformational variety in the polyglutamine expanded mutant than wildtype exon 1. Our data provide a foundation for future functional and drug discovery studies targeting Huntington's disease and illuminate the structural consequences of HTT polyglutamine expansion.
External linksCommun Biol / PubMed:34880419 / PubMed Central
MethodsEM (single particle)
Resolution2.6 Å
Structure data

22106

6x9o

EMDB-22106, PDB-6x9o:
High resolution cryoEM structure of huntingtin in complex with HAP40
Method: EM (single particle) / Resolution: 2.6 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / Huntingtin / HTT / 40-kDa huntingtin-associated protein / HAP40 / Structural Genomics / Structural Genomics Consortium / SGC

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