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TitleDelineation of functional subdomains of Huntingtin protein and their interaction with HAP40.
Journal, issue, pagesStructure, Vol. 31, Issue 9, Page 1121-11131.e6, Year 2023
Publish dateSep 7, 2023
AuthorsMatthew G Alteen / Justin C Deme / Claudia P Alvarez / Peter Loppnau / Ashley Hutchinson / Alma Seitova / Renu Chandrasekaran / Eduardo Silva Ramos / Christopher Secker / Mona Alqazzaz / Erich E Wanker / Susan M Lea / Cheryl H Arrowsmith / Rachel J Harding /
PubMed AbstractThe huntingtin (HTT) protein plays critical roles in numerous cellular pathways by functioning as a scaffold for its many interaction partners and HTT knock out is embryonic lethal. Interrogation of ...The huntingtin (HTT) protein plays critical roles in numerous cellular pathways by functioning as a scaffold for its many interaction partners and HTT knock out is embryonic lethal. Interrogation of HTT function is complicated by the large size of this protein so we studied a suite of structure-rationalized subdomains to investigate the structure-function relationships within the HTT-HAP40 complex. Protein samples derived from the subdomain constructs were validated using biophysical methods and cryo-electron microscopy, revealing they are natively folded and can complex with validated binding partner, HAP40. Derivatized versions of these constructs enable protein-protein interaction assays in vitro, with biotin tags, and in cells, with luciferase two-hybrid assay-based tags, which we use in proof-of-principle analyses to further interrogate the HTT-HAP40 interaction. These open-source biochemical tools enable studies of fundamental HTT biochemistry and biology, will aid the discovery of macromolecular or small-molecule binding partners and help map interaction sites across this large protein.
External linksStructure / PubMed:37390814 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

PDB-8sah:
Huntingtin C-HEAT domain in complex with HAP40
Method: ELECTRON MICROSCOPY / Resolution: 3.2 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / Huntingtin / scaffold / HEAT repeats / Structural Genomics / Structural Genomics Consortium / SGC

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