1H, 13C and 15N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel

被引：2

作者：

Li, Qingxin ^{[1
]}

Ng, Hui Qi ^{[2
]}

Kang, CongBao ^{[2
]}

机构：

[1] Agcy Sci Technol & Res, Inst Chem & Engn Sci, Singapore 138669, Singapore

[2] Agcy Sci Technol & Res, Ctr Expt Therapeut, Singapore 138669, Singapore

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2015年 / 9卷 / 01期

关键词：

Voltage-gated potassium channel; NMR; Cyclic-nucleotide binding domain; Resonance assignment; KCNH channel; HERG; EAG;

D O I：

10.1007/s12104-014-9544-4

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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.

引用

页码：55 / 58

页数：4

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