斑马鱼KCNH通道N端PAS结构域的¹H、¹³C和¹⁵N化学位移归属
¹H, ¹³C and ¹⁵N chemical shift assignments for the N-terminal PAS domain of the KCNH channel from zebrafish.
作者信息
Kim Young Mee, Li Qingxin, Ng Hui Qi, Yoon Ho Sup, Kang CongBao
机构信息
Experimental Therapeutics Centre, Agency for Science, Technology and Research, 31 Biopolis Way Nanos, #03-01, Singapore, 138669, Singapore.
出版信息
Biomol NMR Assign. 2014 Apr;8(1):165-8. doi: 10.1007/s12104-013-9475-5. Epub 2013 Apr 18.
The KCNH channels are voltage-gated potassium channels that play important roles in heart and nerve cells. The N-terminal region of the KCNH channel contains a Per-Arnt-Sim (PAS) domain which is important for the channel gating through interaction with other regions of the channel. To study the solution structure of the N-terminal PAS domain of the KCNH channel from Zebrafish (zNTD), we over-expressed and purified zNTD. We report the resonance assignments for zNTD. The data will allow us to perform structural studies for this domain, which will provide insight into its structural basis for the molecular interaction with other regions of the KCNH channel.
KCNH通道是电压门控钾通道，在心脏和神经细胞中发挥重要作用。KCNH通道的N端区域包含一个Per-Arnt-Sim（PAS）结构域，该结构域通过与通道的其他区域相互作用对通道门控很重要。为了研究斑马鱼KCNH通道N端PAS结构域（zNTD）的溶液结构，我们对zNTD进行了过表达和纯化。我们报告了zNTD的共振归属。这些数据将使我们能够对该结构域进行结构研究，这将为其与KCNH通道其他区域分子相互作用的结构基础提供深入了解。
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