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10.1038/s41467-020-14790-3 http://scihub22266oqcxt.onion/10.1038/s41467-020-14790-3 32081947!7035313!32081947     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 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 1016 Nephropedia Template TP {{tp|p=32081947|t=2020. Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy |pdf=|usr=}}{{32081947}} gab.com Text Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32081947 #FOAvip The secondary active cation-chloride cotransporters (CCCs) utilize the existing Na(+) and/or K(+) gradients to move Cl(-) into or out of cells. NKCC1 is an intensively studied member of the CCC family and plays fundamental roles in regulating trans-epithelial ion movement, cell volume, chloride homeostasis and neuronal excitability. Here, we report a cryo-EM structure of human NKCC1 captured in a partially loaded, inward-open state. NKCC1 assembles into a dimer, with the first ten transmembrane (TM) helices harboring the transport core and TM11-TM12 helices lining the dimer interface. TM1 and TM6 helices break alpha-helical geometry halfway across the lipid bilayer where ion binding sites are organized around these discontinuous regions. NKCC1 may harbor multiple extracellular entryways and intracellular exits, raising the possibility that K(+), Na(+), and Cl(-) ions may traverse along their own routes for translocation. NKCC1 structure provides a blueprint for further probing structure-function relationships of NKCC1 and other CCCs. Twit Text FOAVip Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32081947 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32081947 #FOAvip English Wikipedia <ref>{{Cite pmid|32081947}}</ref> Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy #MMPMID32081947 Yang X; Wang Q; Cao E Nat Commun 2020[Feb]; 11 (1): 1016 PMID32081947show ga The secondary active cation-chloride cotransporters (CCCs) utilize the existing Na(+) and/or K(+) gradients to move Cl(-) into or out of cells. NKCC1 is an intensively studied member of the CCC family and plays fundamental roles in regulating trans-epithelial ion movement, cell volume, chloride homeostasis and neuronal excitability. Here, we report a cryo-EM structure of human NKCC1 captured in a partially loaded, inward-open state. NKCC1 assembles into a dimer, with the first ten transmembrane (TM) helices harboring the transport core and TM11-TM12 helices lining the dimer interface. TM1 and TM6 helices break alpha-helical geometry halfway across the lipid bilayer where ion binding sites are organized around these discontinuous regions. NKCC1 may harbor multiple extracellular entryways and intracellular exits, raising the possibility that K(+), Na(+), and Cl(-) ions may traverse along their own routes for translocation. NKCC1 structure provides a blueprint for further probing structure-function relationships of NKCC1 and other CCCs. |Binding Sites[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Ion Transport[MESH] |Models, Molecular[MESH] |Protein Conformation[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Structure, Quaternary[MESH] |Recombinant Proteins/chemistry/genetics[MESH] |Single Molecule Imaging[MESH]Structure of the human cation-chloride cotransporter NKCC1 determined (epmc).pdf DeepDyve Pubget Overpricing