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10.1126/science.aaf8070 http://scihub22266oqcxt.onion/10.1126/science.aaf8070 C5477842!5477842!27516594     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2016 ; 353 (6300): 664-9 Nephropedia Template TP {{tp|p=27516594|t=2016. Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism |pdf=|usr=}}{{27516594}} gab.com Text Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=27516594 #FOAvip Voltage-gated potassium channels (Kv) are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4?S5 linker, to the potassium pore. We determined the single-particle cryo-EM structure of mammalian Kv10.1 or Eag1, bound to the channel inhibitor calmodulin, at 3.78Å resolution. Unlike previous Kv structures, the S4?S5 linker of Eag1 is a 5-residue loop and the transmembrane segments are not domain swapped, suggesting an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4?S5 linker allows calmodulin to bind to the intracellular domains and close the potassium pore independent of voltage sensor position. The structure reveals an alternative gating mechanism for Kv channels and provides a template to further understand the gating properties of Eag1 and related channels. Twit Text FOAVip Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism ????Science http://www.kidney.de/pget.php?&tw=1&pmid=27516594 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27516594 #FOAvip English Wikipedia <ref>{{Cite pmid|27516594}}</ref> Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism #MMPMID27516594 Whicher JR; MacKinnon R Science 2016[Aug]; 353 (6300): 664-9 PMID27516594show ga Voltage-gated potassium channels (Kv) are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4?S5 linker, to the potassium pore. We determined the single-particle cryo-EM structure of mammalian Kv10.1 or Eag1, bound to the channel inhibitor calmodulin, at 3.78Å resolution. Unlike previous Kv structures, the S4?S5 linker of Eag1 is a 5-residue loop and the transmembrane segments are not domain swapped, suggesting an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4?S5 linker allows calmodulin to bind to the intracellular domains and close the potassium pore independent of voltage sensor position. The structure reveals an alternative gating mechanism for Kv channels and provides a template to further understand the gating properties of Eag1 and related channels. äStructure of the voltage-gated K+ channel Eag1 reveals an alternative (epmc).pdf DeepDyve Pubget Overpricing