Published December 3, 2018
| Version v1
Dataset
Open
Coexpression and purification of HTT domains with HAP40 - 2018/12/03
Authors/Creators
- 1. Structural Genomics Consortium, University of Toronto
Description
Project: High resolution structural analysis of purified HTT proteins
Experiment: Coexpression and purification of HTT domains with HAP40
Date completed: 2018/12/03
Rationale: HTT domain fragments are challenging to express and purify. However, the full-length protein sample was shown to have superior biophysical characteristics when coexpressed and purified with HAP40. As HAP40 has an extensive interaction surface with HTT, it could be possible to copurify domain fragments of HTT with HAP40, stabilizing the individual HEAT domains.
Notes
Dr. Harding is the recipient of the Huntington's Disease Society of America Berman Topper Career Development Fellowship which funds and supports this research, in addition to generous funding from the CHDI Foundation and the Huntington Society of Canada. The SGC is a registered charity (number 1097737) that receives funds from AbbVie, Bayer Pharma AG, Boehringer Ingelheim, Canada Foundation for Innovation, Eshelman Institute for Innovation, Genome Canada through Ontario Genomics Institute [OGI-055], Innovative Medicines Initiative (EU/EFPIA) [ULTRA-DD grant no. 115766], Janssen, Merck KGaA, Darmstadt, Germany, MSD, Novartis Pharma AG, Ontario Ministry of Research, Innovation and Science (MRIS), Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome.