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10.4161/chan.1.6.5760 http://scihub22266oqcxt.onion/10.4161/chan.1.6.5760 18690045!2847495!18690045     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Channels+(Austin) 2007 ; 1 (6): 429-37 Nephropedia Template TP {{tp|p=18690045|t=2007. Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating |pdf=|usr=}}{{18690045}} gab.com Text Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating JO: Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=18690045 #FOAvip HERG (KCNH2) and ether-a-go-go (eag) (KCNH1) are members of the same subfamily of voltage-gated K+ channels. In eag, voltage-dependent activation is significantly slowed by extracellular divalent cations. To exert this effect, ions bind to a site located between transmembrane segments S2 and S3 in the voltage sensor domain where they interact with acidic residues that are conserved only among members of the eag subfamily. In HERG channels, extracellular divalent ions significantly accelerate deactivation. To investigate the ionbinding site in HERG, acidic residues in S2 and S3 were neutralized singly or in pairs to alanine, and the functional effects of extracellular Mg(2+) were characterized in Xenopus oocytes. To modulate deactivation kinetics in HERG, divalent cations interact with eag subfamily-specific acidic residues (D460 and D509) and also with an acidic residue in S2 (D456) that is widely conserved in the voltage-gated channel superfamily. In contrast, the analogous widely-conserved residue does not contribute to the ion-binding site that modulates activation kinetics in eag. We propose that structural differences between the ion-binding sites in the eag and HERG voltage sensors contribute to the differential regulation of activation and deactivation gating in these channels. A previously proposed model for S4 conformational changes during voltagedependent activation can account for the differential regulation of gating seen in eag and HERG. Twit Text FOAVip Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating ????Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=18690045 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18690045 #FOAvip English Wikipedia <ref>{{Cite pmid|18690045}}</ref> Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating #MMPMID18690045 Lin MC; Papazian DM Channels (Austin) 2007[Nov]; 1 (6): 429-37 PMID18690045show ga HERG (KCNH2) and ether-a-go-go (eag) (KCNH1) are members of the same subfamily of voltage-gated K+ channels. In eag, voltage-dependent activation is significantly slowed by extracellular divalent cations. To exert this effect, ions bind to a site located between transmembrane segments S2 and S3 in the voltage sensor domain where they interact with acidic residues that are conserved only among members of the eag subfamily. In HERG channels, extracellular divalent ions significantly accelerate deactivation. To investigate the ionbinding site in HERG, acidic residues in S2 and S3 were neutralized singly or in pairs to alanine, and the functional effects of extracellular Mg(2+) were characterized in Xenopus oocytes. To modulate deactivation kinetics in HERG, divalent cations interact with eag subfamily-specific acidic residues (D460 and D509) and also with an acidic residue in S2 (D456) that is widely conserved in the voltage-gated channel superfamily. In contrast, the analogous widely-conserved residue does not contribute to the ion-binding site that modulates activation kinetics in eag. We propose that structural differences between the ion-binding sites in the eag and HERG voltage sensors contribute to the differential regulation of activation and deactivation gating in these channels. A previously proposed model for S4 conformational changes during voltagedependent activation can account for the differential regulation of gating seen in eag and HERG. |Amino Acid Sequence[MESH] |Animals[MESH] |Binding Sites[MESH] |Cations[MESH] |ERG1 Potassium Channel[MESH] |Ether-A-Go-Go Potassium Channels/*chemistry/metabolism[MESH] |Ions/*chemistry[MESH] |Kinetics[MESH] |Magnesium/chemistry[MESH] |Molecular Sequence Data[MESH] |Oocytes/metabolism[MESH] |Potassium Channels, Voltage-Gated/*chemistry[MESH] |Protein Binding[MESH] |Sequence Homology, Amino Acid[MESH]Differences between ion binding to eag and HERG voltage sensors contri(epmc).pdf DeepDyve Pubget Overpricing