Abstract
The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, considering possible use as a drug target. We produced H-2, N-15, C-13 labelled-Nurr1 to generate the backbone amide NH, carbonyl C', C-alpha and C-beta assignments. About 84.0% of residues could be assigned. Most of the 37 missing assignments fall in 3 regions of the protein. Two of these surround a putative ligand-binding region of Nurr1, suggesting that this region of the protein is flexible, despite the ligand-binding pocket being filled with hydrophobic side-chains from residues surrounding the ligand binding pocket.
Original language | English |
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Pages (from-to) | 101-105 |
Number of pages | 5 |
Journal | Biomolecular NMR Assignments |
Volume | 4 |
Issue number | 1 |
Early online date | 19 Mar 2010 |
DOIs | |
Publication status | Published - 1 Apr 2010 |
Keywords
- NR4A nuclear receptors
- Orphan nuclear receptor
- Parkinson's disease
- Nurr1
- NMR