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10.1152/ajpcell.00465.2019 http://scihub22266oqcxt.onion/10.1152/ajpcell.00465.2019 31747317!7052613!31747317     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Physiol+Cell+Physiol 2020 ; 318 (2): C225-C237 Nephropedia Template TP {{tp|p=31747317|t=2020. Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physiology of cation-chloride cotransporters |pdf=|usr=}}{{31747317}} gab.com Text Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physiology of cation-chloride cotransporters JO: Am J Physiol Cell Physiol http://www.kidney.de/pget.php?&tw=1&pmid=31747317 #FOAvip New milestones have been reached in the field of cation-Cl(-) cotransporters with the recently released cryo-electron microscopy (EM) structures of the Danio rerio (zebrafish) Na(+)-K(+)-2Cl(-) cotransporter (DrNKCC1) and the human K(+)-Cl(-) cotransporter (hKCC1). In this review we provide a brief timeline that identifies the multiple breakthroughs in the field of solute carrier 12 transporters that led to the structure resolution of two of its key members. While cation-Cl(-) cotransporters share the overall architecture of carriers belonging to the amino acid-polyamine-organocation (APC) superfamily and some of their substrate binding sites, several new insights are gained from the two individual structures. A first major feature relates to the largest extracellular domain between transmembrane domain (TMD) 5 and TMD6 of KCC1, which stabilizes the dimer and forms a cap that likely participates in extracellular gating. A second feature is the conservation of the K(+) and Cl(-) binding sites in both structures and evidence of an unexpected second Cl(-) coordination site in the KCC1 structure. Structural data are discussed in the context of previously published studies that examined the basic and kinetics properties of these cotransport mechanisms. A third characteristic is the evidence of an extracellular gate formed by conserved salt bridges between charged residues located toward the end of TMD3 and TMD4 in both transporters and the existence of an additional neighboring bridge in the hKCC1 structure. A fourth feature of these newly solved structures relates to the multiple points of contacts between the monomer forming the cotransporter homodimer units. These involve the TMDs, the COOH-terminal domains, and the large extracellular loop for hKCC1. Twit Text FOAVip Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physiology of cation-chloride cotransporters ????Am J Physiol Cell Physiol http://www.kidney.de/pget.php?&tw=1&pmid=31747317 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=31747317 #FOAvip English Wikipedia <ref>{{Cite pmid|31747317}}</ref> Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physiology of cation-chloride cotransporters #MMPMID31747317 Delpire E; Guo J Am J Physiol Cell Physiol 2020[Feb]; 318 (2): C225-C237 PMID31747317show ga New milestones have been reached in the field of cation-Cl(-) cotransporters with the recently released cryo-electron microscopy (EM) structures of the Danio rerio (zebrafish) Na(+)-K(+)-2Cl(-) cotransporter (DrNKCC1) and the human K(+)-Cl(-) cotransporter (hKCC1). In this review we provide a brief timeline that identifies the multiple breakthroughs in the field of solute carrier 12 transporters that led to the structure resolution of two of its key members. While cation-Cl(-) cotransporters share the overall architecture of carriers belonging to the amino acid-polyamine-organocation (APC) superfamily and some of their substrate binding sites, several new insights are gained from the two individual structures. A first major feature relates to the largest extracellular domain between transmembrane domain (TMD) 5 and TMD6 of KCC1, which stabilizes the dimer and forms a cap that likely participates in extracellular gating. A second feature is the conservation of the K(+) and Cl(-) binding sites in both structures and evidence of an unexpected second Cl(-) coordination site in the KCC1 structure. Structural data are discussed in the context of previously published studies that examined the basic and kinetics properties of these cotransport mechanisms. A third characteristic is the evidence of an extracellular gate formed by conserved salt bridges between charged residues located toward the end of TMD3 and TMD4 in both transporters and the existence of an additional neighboring bridge in the hKCC1 structure. A fourth feature of these newly solved structures relates to the multiple points of contacts between the monomer forming the cotransporter homodimer units. These involve the TMDs, the COOH-terminal domains, and the large extracellular loop for hKCC1. |Amino Acid Sequence[MESH] |Animals[MESH] |Cations/*chemistry[MESH] |Chlorides/*chemistry[MESH] |Cryoelectron Microscopy/methods[MESH] |Humans[MESH] |K Cl- Cotransporters[MESH] |Solute Carrier Family 12, Member 2/*chemistry[MESH]Cryo-EM structures of DrNKCC1 and hKCC1: a new milestone in the physio(epmc).pdf DeepDyve Pubget Overpricing