KCNH通道环核苷酸结合同源结构域的(1)H、(13)C和(15)N化学位移归属
(1)H, (13)C and (15)N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel.
作者信息
Li Qingxin, Ng Hui Qi, Kang CongBao
机构信息
Institute of Chemical & Engineering Sciences, Agency for Science, Technology and Research, Singapore, Singapore.
出版信息
Biomol NMR Assign. 2015 Apr;9(1):55-8. doi: 10.1007/s12104-014-9544-4. Epub 2014 Jan 11.
The KCNH family of ion channels plays important roles in heart and nerve cells. The C-terminal region of the KCNH channel contains a cyclic-nucleotide binding homology domain (CNBHD) which is important for channel gating through interaction with the eag domain. To study the solution structure of CNBHD of the KCNH channel of zebrafish, we over-expressed and purified this domain from E. coli. We report the resonance assignments of the CNBHD. The assignments will allow us to perform structural and dynamic studies for this domain, which will shed light on its role in channel gating.
离子通道的KCNH家族在心脏和神经细胞中发挥着重要作用。KCNH通道的C末端区域包含一个环核苷酸结合同源结构域（CNBHD），该结构域通过与eag结构域相互作用对通道门控很重要。为了研究斑马鱼KCNH通道CNBHD的溶液结构，我们从大肠杆菌中过表达并纯化了该结构域。我们报告了CNBHD的共振归属。这些归属将使我们能够对该结构域进行结构和动力学研究，这将有助于阐明其在通道门控中的作用。
Zotero 插件