Gayen Shovanlal, Li Qingxin, Kang CongBao
Experimental Therapeutics Centre, Agency for Science, Technology and Research (A(∗)STAR), Singapore 138669, Singapore.
Institute of Chemical & Engineering Sciences, Agency for Science, Technology and Research (A(∗)STAR), Singapore, Singapore.
Biochem Biophys Res Commun. 2015 Jan 2;456(1):410-4. doi: 10.1016/j.bbrc.2014.11.097. Epub 2014 Dec 2.
KCNQ1 plays important roles in the cardiac action potential and consists of an N-terminal domain, a voltage-sensor domain, a pore domain and a C-terminal domain. KCNQ1 is a voltage-gated potassium channel and its channel activity is regulated by membrane potentials. The linker between transmembrane helices 4 and 5 (S4-S5 linker) is important for transferring the conformational changes from the voltage-sensor domain to the pore domain. In this study, the structure of the S4-S5 linker of KCNQ1 was investigated by solution NMR, circular dichroism and fluorescence spectroscopic studies. The S4-S5 linker adopted a helical structure in detergent micelles. The W248 may interact with the cell membrane.
KCNQ1在心脏动作电位中发挥重要作用，由一个N端结构域、一个电压感受器结构域、一个孔道结构域和一个C端结构域组成。KCNQ1是一种电压门控钾通道，其通道活性受膜电位调节。跨膜螺旋4和5之间的连接子（S4-S5连接子）对于将构象变化从电压感受器结构域传递到孔道结构域很重要。在本研究中，通过溶液核磁共振、圆二色光谱和荧光光谱研究对KCNQ1的S4-S5连接子结构进行了研究。S4-S5连接子在去污剂胶束中采用螺旋结构。W248可能与细胞膜相互作用。
