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10.7554/eLife.24149 http://scihub22266oqcxt.onion/10.7554/eLife.24149 C5344670!5344670!28092267     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28092267|t=2017. Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating |pdf=|usr=}}{{28092267}} gab.com Text Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28092267 #FOAvip KATP channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic ?-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6 Å resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity.DOI:http://dx.doi.org/10.7554/eLife.24149.001 Twit Text FOAVip Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28092267 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28092267 #FOAvip English Wikipedia <ref>{{Cite pmid|28092267}}</ref> Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating #MMPMID28092267 Martin GM; Yoshioka C; Rex EA; Fay JF; Xie Q; Whorton MR; Chen JZ; Shyng SL eLife 2017[]; 6 (ä): ä PMID28092267show ga KATP channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic ?-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6 Å resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity.DOI:http://dx.doi.org/10.7554/eLife.24149.001 äCryo-EM structure of the ATP-sensitive potassium channel illuminates m(epmc).pdf DeepDyve Pubget Overpricing