Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81668
Title: Insight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channel
Authors: Li, Qingxin
Ng, Hui Qi
Yoon, Ho Sup
Kang, CongBao
Keywords: hERG
Cyclic nucleotide-binding homology domain
Issue Date: 2014
Source: Li, Q., Ng, H. Q., Yoon, H. S., & Kang, C. (2014). Insight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channel. FEBS Letters, 588(17), 2782-2788.
Series/Report no.: FEBS Letters
Abstract: The gating of the hERG channel is regulated by its eag domain through molecular interaction with either the cyclic nucleotide-binding homology domain (CNBHD) or the linker between transmembrane segments 4 and 5. Our NMR study on the purified CNBHD demonstrated that it contains nine β-strands and does not bind cAMP. We show that the eag domain binds to the CBND through an interface containing several disease-associated mutations. The N-terminal cap domain and R56 in the eag domain are important for the interaction with the CNBHD. Residues from the CNBHD that were affected by the interaction with the eag domain were also identified. A R56Q mutation does not cause major structural changes in the eag domain and showed reduced interaction with the CNBHD.
URI: https://hdl.handle.net/10356/81668
http://hdl.handle.net/10220/40916
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2014.05.056
Rights: © 2014 Federation of European Biochemical Societies (Published by Elsevier B.V.).
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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