Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein
- 影响因子：
0.0
- 发表刊物：
Int J Biol Macromol.
- 摘要：
The structure of a ubiquitin-like protein, small ubiquitin-related modifier-1 (SUMO-1), was earlier determined using homonuclear nuclear magnetic resonance (NMR) spectroscopy, since the spectral quality of the protein was not suitable for heteronuclear NMR data collection. In this study, a slightly different construct of the SUMO-1 gene was used for protein over-expression. The protein purified from this construct showed high spectral qualities, therefore, multi-dimensional heteronuclear NMR data for a dynamic study and structural determination were acquired. The structure of SUMO-1 obtained in this study differs in several respects from the structure obtained from homonuclear NMR data. Furthermore, structural differences were observed between the new SUMO-1 and ubiquitin structures. These differences may be important for SUMO-1-specific recognition in cells. Additionally, relaxation parameters indicate that SUMO-1 undergoes highly anisotropic tumbling in solution and that the long amino (N)-terminal sequence of SUMO-1 is highly dynamic with increasing flexibility towards the end.
- 论文类型：
期刊论文
- 卷号：
28
- 期号：
3
- 页面范围：
227-234
- 是否译文：
否
- 发表时间：
2011-03-14
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Jin Changwen
- 通讯作者：
Liao Xiubei
- 全部作者：
Shen Zhiyuan,Shiyanova Tatanya
