title: (1)H, (13)C and (15)N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel.
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.
authors.affiliation: Institute of Chemical & Engineering Sciences, Agency for Science, Technology and Research, Singapore, Singapore.
authors.forename: Qingxin
authors.initials: Q
authors.lastname: Li
authors.forename: Hui Qi
authors.initials: HQ
authors.lastname: Ng
authors.forename: CongBao
authors.initials: C
authors.lastname: Kang
mesh_terms: D000818:Animals; D051638:Ether-A-Go-Go Potassium Channels / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009712:Nucleotides, Cyclic / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D015027:Zebrafish; D029961:Zebrafish Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D051638:Ether-A-Go-Go Potassium Channels; D009712:Nucleotides, Cyclic; D029961:Zebrafish Proteins