Crystal structure of the PAS domain of the hEAG potassium channel

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• 作者：Xue Tang ; Juan Shao and Xiaohong Qin
• 关键词：KCNH channels ; PAS domain ; ether-à ; -go-go channel ; hEAG potassium chanels
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：August 2016
• 年：2016
• 卷：72
• 期：8
• 页码：578-585
• 全文大小：1672K
• ISSN：1744-3091

文摘

KCNH voltage-gated potassium channels play critical roles in regulating cellular functions. The channel is composed of four subunits, each of which contains six transmembrane helices forming the central pore. The cytoplasmic parts of the subunits present a Per–Arnt–Sim (PAS) domain at the N-terminus and a cyclic nucleotide-binding homology domain at the C-terminus. PAS domains are conserved from prokaryotes to eukaryotes and are involved in sensing signals and cellular responses. To better understand the functional roles of PAS domains in KCNH channels, the structure of this domain from the human ether-à-go-go channel (hEAG channel) was determined. By comparing it with the structures of the Homo sapiens EAG-related gene (hERG) channel and the Drosophila EAG-like K⁺ (dELK) channel and analyzing the structural features of the hEAG channel, it was identified that a hydrophobic patch on the β-sheet may mediate interaction between the PAS domain and other regions of the channel to regulate its functions.