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10.1073/pnas.1620799114 http://scihub22266oqcxt.onion/10.1073/pnas.1620799114 C5358357!5358357!28242691     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11): 2904-9 Nephropedia Template TP {{tp|p=28242691|t=2017. Specific phospholipid binding to Na,K-ATPase at two distinct sites |pdf=|usr=}}{{28242691}} gab.com Text Specific phospholipid binding to Na,K-ATPase at two distinct sites JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28242691 #FOAvip Activity and structural integrity of membrane proteins can be regulated by physical properties of the bilayer or specific lipid?protein interactions. This work shows that key properties of the Na,K-ATPase are modulated independently by specific binding of 18:0/18:1 phosphatidylserine (PS) and 18:0/20:4 phosphatidylcholine (PC) in the absence of a bilayer. PS stabilizes the protein, and PC/ phosphatidylethanolamine (PE) stimulates Na,K-ATPase activity. We characterized effects of both types of phospholipids by kinetic approaches, mutant analyses, and native MS. Modulation of Na,K-ATPase function by PS and PC/PE is defined by the phospholipid structural specificity, binding stoichiometry within two specific binding sites, and the kinetic mechanism. We provide detailed mechanistic insights, potentially with important implications for physiological regulation of active Na and K transport. Twit Text FOAVip Specific phospholipid binding to Na,K-ATPase at two distinct sites ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28242691 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28242691 #FOAvip English Wikipedia <ref>{{Cite pmid|28242691}}</ref> Specific phospholipid binding to Na,K-ATPase at two distinct sites #MMPMID28242691 Habeck M; Kapri-Pardes E; Sharon M; Karlish SJD Proc Natl Acad Sci U S A 2017[Mar]; 114 (11): 2904-9 PMID28242691show ga Activity and structural integrity of membrane proteins can be regulated by physical properties of the bilayer or specific lipid?protein interactions. This work shows that key properties of the Na,K-ATPase are modulated independently by specific binding of 18:0/18:1 phosphatidylserine (PS) and 18:0/20:4 phosphatidylcholine (PC) in the absence of a bilayer. PS stabilizes the protein, and PC/ phosphatidylethanolamine (PE) stimulates Na,K-ATPase activity. We characterized effects of both types of phospholipids by kinetic approaches, mutant analyses, and native MS. Modulation of Na,K-ATPase function by PS and PC/PE is defined by the phospholipid structural specificity, binding stoichiometry within two specific binding sites, and the kinetic mechanism. We provide detailed mechanistic insights, potentially with important implications for physiological regulation of active Na and K transport. äSpecific phospholipid binding to Na,K-ATPase at two distinct sites (epmc).pdf DeepDyve Pubget Overpricing