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10.7554/eLife.36615 http://scihub22266oqcxt.onion/10.7554/eLife.36615 C5951680!5951680!29717981     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2018 ; 7 (ä): ä Nephropedia Template TP {{tp|p=29717981|t=2018. Electron cryo-microscopy structure of the canonical TRPC4 ion channel |pdf=|usr=}}{{29717981}} gab.com Text Electron cryo-microscopy structure of the canonical TRPC4 ion channel JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=29717981 #FOAvip Canonical transient receptor channels (TRPC) are non-selective cation channels. They are involved in receptor-operated Ca2+ signaling and have been proposed to act as store-operated channels (SOC). Their malfunction is related to cardiomyopathies and their modulation by small molecules has been shown to be effective against renal cancer cells. The molecular mechanism underlying the complex activation and regulation is poorly understood. Here, we report the electron cryo-microscopy structure of zebrafish TRPC4 in its unliganded (apo), closed state at an overall resolution of 3.6 Å. The structure reveals the molecular architecture of the cation conducting pore, including the selectivity filter and lower gate. The cytoplasmic domain contains two key hubs that have been shown to interact with modulating proteins. Structural comparisons with other TRP channels give novel insights into the general architecture and domain organization of this superfamily of channels and help to understand their function and pharmacology. Twit Text FOAVip Electron cryo-microscopy structure of the canonical TRPC4 ion channel ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=29717981 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29717981 #FOAvip English Wikipedia <ref>{{Cite pmid|29717981}}</ref> Electron cryo-microscopy structure of the canonical TRPC4 ion channel #MMPMID29717981 Vinayagam D; Mager T; Apelbaum A; Bothe A; Merino F; Hofnagel O; Gatsogiannis C; Raunser S eLife 2018[]; 7 (ä): ä PMID29717981show ga Canonical transient receptor channels (TRPC) are non-selective cation channels. They are involved in receptor-operated Ca2+ signaling and have been proposed to act as store-operated channels (SOC). Their malfunction is related to cardiomyopathies and their modulation by small molecules has been shown to be effective against renal cancer cells. The molecular mechanism underlying the complex activation and regulation is poorly understood. Here, we report the electron cryo-microscopy structure of zebrafish TRPC4 in its unliganded (apo), closed state at an overall resolution of 3.6 Å. The structure reveals the molecular architecture of the cation conducting pore, including the selectivity filter and lower gate. The cytoplasmic domain contains two key hubs that have been shown to interact with modulating proteins. Structural comparisons with other TRP channels give novel insights into the general architecture and domain organization of this superfamily of channels and help to understand their function and pharmacology. äElectron cryo-microscopy structure of the canonical TRPC4 ion channel (epmc).pdf DeepDyve Pubget Overpricing