Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81804
Title: Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel
Authors: Li, Qingxin
Ng, Hui Qi
Yoon, Ho Sup
Kang, Congbao
Keywords: Voltage-gated potassium channel
Cyclic-nucleotide binding domain
Issue Date: 2014
Source: Li, Q., Ng, H. Q., Yoon, H. S., & Kang, C. (2014). Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel. Journal of Structural Biology, 186(1), 68-74.
Series/Report no.: Journal of Structural Biology
Abstract: The carboxy-terminal region of the KCNH family of potassium channels contains a cyclic-nucleotide binding homology domain (CNBHD) that is important for channel gating and trafficking. The solution structure of the CNBHD of the KCNH potassium of zebrafish was determined using solution NMR spectroscopy. This domain exists as a monomer under solution conditions and adopts a similar fold to that determined by X-ray crystallography. The CNBHD does not bind cAMP because residue Y740 blocks the entry of cyclic-nucleotide to the binding pocket. Relaxation results show that the CNBHD is rigid except that some residues in the loop between β6 and β7 are flexible. Our results will be useful to understand the gating mechanism of KCNH family members through the CNBHD.
URI: https://hdl.handle.net/10356/81804
http://hdl.handle.net/10220/40960
ISSN: 1047-8477
DOI: 10.1016/j.jsb.2014.03.008
Rights: © 2014 Elsevier.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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