Michiels Paul, Atkins Karen, Ludwig Christian, Whittaker Sara, van Dongen Maria, Günther Ulrich
Solvay Pharmaceuticals Research Laboratories, Hannover, Germany.
Biomol NMR Assign. 2010 Apr;4(1):101-5. doi: 10.1007/s12104-010-9210-4. Epub 2010 Mar 19.
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 (2)H, (15)N, (13)C 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.
孤儿核受体Nurr1与包括帕金森病和精神分裂症在内的多种病症有关。因此，考虑到其可能作为药物靶点的用途，研究其与其他蛋白质的相互作用（可能由小分子介导）具有重要意义。我们制备了（2）H、（15）N、（13）C标记的Nurr1，以确定主链酰胺NH、羰基C'、Cα和Cβ的归属。约84.0%的残基可以被归属。37个未归属的残基大多位于蛋白质的3个区域。其中两个区域围绕着Nurr1的一个假定配体结合区域，这表明尽管配体结合口袋被来自配体结合口袋周围残基的疏水侧链填满，但该蛋白质区域是灵活的。
