Referenced in: none

Automatically associated channels: Kv10.1

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

Authors: Qingxin Li, Hui Qi Ng, Congbao Kang

Journal, date & volume: Biomol NMR Assign, 2014 Jan 11 , ,

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/24414223

Abstract
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.