Structural highlights
Publication Abstract from PubMed
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 beta6 and beta7 are flexible. Our results will be useful to understand the gating mechanism of KCNH family members through the CNBHD.
Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel.,Li Q, Ng HQ, Yoon HS, Kang C J Struct Biol. 2014 Mar 14. pii: S1047-8477(14)00061-6. doi:, 10.1016/j.jsb.2014.03.008. PMID:24632450[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Q, Ng HQ, Yoon HS, Kang C. Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel. J Struct Biol. 2014 Mar 14. pii: S1047-8477(14)00061-6. doi:, 10.1016/j.jsb.2014.03.008. PMID:24632450 doi:http://dx.doi.org/10.1016/j.jsb.2014.03.008
