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kcnh mutation

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https://www.readbyqxmd.com/read/27025590/structure-of-the-cyclic-nucleotide-binding-homology-domain-of-the-herg-channel-and-its-insight-into-type-2-long-qt-syndrome
#1
Yan Li, Hui Qi Ng, Qingxin Li, CongBao Kang
The human ether-à-go-go related gene (hERG) channel is crucial for the cardiac action potential by contributing to the fast delayed-rectifier potassium current. Mutations in the hERG channel result in type 2 long QT syndrome (LQT2). The hERG channel contains a cyclic nucleotide-binding homology domain (CNBHD) and this domain is required for the channel gating though molecular interactions with the eag domain. Here we present solution structure of the CNBHD of the hERG channel. The structural study reveals that the CNBHD adopts a similar fold to other KCNH channels...
2016: Scientific Reports
https://www.readbyqxmd.com/read/25333352/the-eag-domain-regulates-the-voltage-dependent-inactivation-of-rat-eag1-k-channels
#2
Ting-Feng Lin, Guey-Mei Jow, Hsin-Yu Fang, Ssu-Ju Fu, Hao-Han Wu, Mei-Miao Chiu, Chung-Jiuan Jeng
Eag (Kv10) and Erg (Kv11) belong to two distinct subfamilies of the ether-à-go-go K+ channel family (KCNH). While Erg channels are characterized by an inward-rectifying current-voltage relationship that results from a C-type inactivation, mammalian Eag channels display little or no voltage-dependent inactivation. Although the amino (N)-terminal region such as the eag domain is not required for the C-type inactivation of Erg channels, an N-terminal deletion in mouse Eag1 has been shown to produce a voltage-dependent inactivation...
2014: PloS One
https://www.readbyqxmd.com/read/24204727/c-terminal-%C3%AE-9-strand-of-the-cyclic-nucleotide-binding-homology-domain-stabilizes-activated-states-of-kv11-1-channels
#3
Chai Ann Ng, Ying Ke, Matthew D Perry, Peter S Tan, Adam P Hill, Jamie I Vandenberg
Kv11.1 potassium channels are important for regulation of the normal rhythm of the heartbeat. Reduced activity of Kv11.1 channels causes long QT syndrome type 2, a disorder that increases the risk of cardiac arrhythmias and sudden cardiac arrest. Kv11.1 channels are members of the KCNH subfamily of voltage-gated K(+) channels. However, they also share many similarities with the cyclic nucleotide gated ion channel family, including having a cyclic nucleotide-binding homology (cNBH) domain. Kv11.1 channels, however, are not directly regulated by cyclic nucleotides...
2013: PloS One
https://www.readbyqxmd.com/read/23975098/the-structural-mechanism-of-kcnh-channel-regulation-by-the-eag-domain
#4
Yoni Haitin, Anne E Carlson, William N Zagotta
The KCNH voltage-dependent potassium channels (ether-à-go-go, EAG; EAG-related gene, ERG; EAG-like channels, ELK) are important regulators of cellular excitability and have key roles in diseases such as cardiac long QT syndrome type 2 (LQT2), epilepsy, schizophrenia and cancer. The intracellular domains of KCNH channels are structurally distinct from other voltage-gated channels. The amino-terminal region contains an eag domain, which is composed of a Per-Arnt-Sim (PAS) domain and a PAS-cap domain, whereas the carboxy-terminal region contains a cyclic nucleotide-binding homology domain (CNBHD), which is connected to the pore through a C-linker domain...
September 19, 2013: Nature
https://www.readbyqxmd.com/read/23801759/structure-of-the-c-terminal-region-of-an-erg-channel-and-functional-implications
#5
Tinatin I Brelidze, Elena C Gianulis, Frank DiMaio, Matthew C Trudeau, William N Zagotta
The human ether-à-go-go-related gene (hERG) encodes a K(+) channel crucial for repolarization of the cardiac action potential. EAG-related gene (ERG) channels contain a C-terminal cyclic nucleotide-binding homology domain coupled to the pore of the channel by a C-linker. Here, we report the structure of the C-linker/cyclic nucleotide-binding homology domain of a mosquito ERG channel at 2.5-Å resolution. The structure reveals that the region expected to form the cyclic nucleotide-binding pocket is negatively charged and is occupied by a short β-strand, referred to as the intrinsic ligand, explaining the lack of direct regulation of ERG channels by cyclic nucleotides...
July 9, 2013: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/23555008/structural-properties-of-pas-domains-from-the-kcnh-potassium-channels
#6
Ricardo Adaixo, Carol A Harley, Artur F Castro-Rodrigues, João H Morais-Cabral
KCNH channels form an important family of voltage gated potassium channels. These channels include a N-terminal Per-Arnt-Sim (PAS) domain with unknown function. In other proteins PAS domains are implicated in cellular responses to environmental queues through small molecule binding or involvement in signaling cascades. To better understand their role we characterized the structural properties of several channel PAS domains. We determined high resolution structures of PAS domains from the mouse EAG (mEAG), drosophila ELK (dELK) and human ERG (hERG) channels and also of the hERG domain without the first nine amino acids...
2013: PloS One
https://www.readbyqxmd.com/read/23440277/flavonoid-regulation-of-eag1-channels
#7
Anne E Carlson, Tinatin I Brelidze, William N Zagotta
The voltage-gated, K(+)-selective ether á go-go 1 (EAG1) channel is expressed throughout the brain where it is thought to regulate neuronal excitability. Besides its normal physiological role in the brain, EAG1 is abnormally expressed in several cancer cell types and promotes tumor progression. Like all other channels in the KCNH family, EAG1 channels have a large intracellular carboxy-terminal region that shares structural similarity with cyclic nucleotide-binding homology domains (CNBHDs). EAG1 channels, however, are not regulated by the direct binding of cyclic nucleotides and have no known endogenous ligands...
March 2013: Journal of General Physiology
https://www.readbyqxmd.com/read/22230959/structure-of-the-carboxy-terminal-region-of-a-kcnh-channel
#8
Tinatin I Brelidze, Anne E Carlson, Banumathi Sankaran, William N Zagotta
The KCNH family of ion channels, comprising ether-à-go-go (EAG), EAG-related gene (ERG), and EAG-like (ELK) K(+)-channel subfamilies, is crucial for repolarization of the cardiac action potential, regulation of neuronal excitability and proliferation of tumour cells. The carboxy-terminal region of KCNH channels contains a cyclic-nucleotide-binding homology domain (CNBHD) and C-linker that couples the CNBHD to the pore. The C-linker/CNBHD is essential for proper function and trafficking of ion channels in the KCNH family...
January 26, 2012: Nature
https://www.readbyqxmd.com/read/20566482/abnormal-repolarization-dynamics-revealed-in-exercise-test-in-long-qt-syndrome-mutation-carriers-with-normal-resting-qt-interval
#9
Anna-Mari Hekkala, Matti Viitasalo, Heikki Väänänen, Heikki Swan, Lauri Toivonen
AIMS: The identification of affected family members with long QT syndrome (LQTS) is often difficult due to their normal-or only marginally lengthened-QT interval duration. We examined whether physical exercise test could increase the ability to detect the mutation carrier status in phenotypically normal LQTS family members. METHODS AND RESULTS: Sixty-six subjects were included: 15 were carriers of KCNQ1 (LQT1); 15 of KCNH(2) (LQT2); and 9 of SCN5A (LQT3) gene mutations with no, or borderline, QT lengthening; and 27 were healthy controls...
September 2010: Europace: European Pacing, Arrhythmias, and Cardiac Electrophysiology
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