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10.1021/bi5006915 http://scihub22266oqcxt.onion/10.1021/bi5006915 C4131901!4131901!25073009     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochemistry 2014 ; 53 (31): 5140-9 Nephropedia Template TP {{tp|p=25073009|t=2014. Mechanistic Insights into the Allosteric Modulation of Opioid Receptors by Sodium Ions |pdf=|usr=}}{{25073009}} gab.com Text Mechanistic Insights into the Allosteric Modulation of Opioid Receptors by Sodium Ions JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=25073009 #FOAvip The idea of sodium ions altering G-protein-coupled receptor (GPCR) ligand binding and signaling was first suggested for opioid receptors (ORs) in the 1970s and subsequently extended to other GPCRs. Recently published ultra-high-resolution crystal structures of GPCRs, including that of the ?-OR subtype, have started to shed light on the mechanism underlying sodium control in GPCR signaling by revealing details of the sodium binding site. Whether sodium accesses different receptor subtypes from the extra- or intracellular sides, following similar or different pathways, is still an open question. Earlier experiments in brain homogenates suggested a differential sodium regulation of ligand binding to the three major OR subtypes, in spite of their high degree of sequence similarity. Intrigued by this possibility, we explored the dynamic nature of sodium binding to ?-OR, ?-OR, and ?-OR by means of microsecond-scale, all-atom molecular dynamics (MD) simulations. Rapid sodium permeation was observed exclusively from the extracellular milieu, and following similar binding pathways in all three ligand-free OR systems, notwithstanding extra densities of sodium observed near nonconserved residues of ?-OR and ?-OR, but not in ?-OR. We speculate that these differences may be responsible for the differential increase in antagonist binding affinity of ?-OR by sodium resulting from specific ligand binding experiments in transfected cells. On the other hand, sodium reduced the level of binding of subtype-specific agonists to all OR subtypes. Additional biased and unbiased MD simulations were conducted using the ?-OR ultra-high-resolution crystal structure as a model system to provide a mechanistic explanation for this experimental observation. Twit Text FOAVip Mechanistic Insights into the Allosteric Modulation of Opioid Receptors by Sodium Ions ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=25073009 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25073009 #FOAvip English Wikipedia <ref>{{Cite pmid|25073009}}</ref> Mechanistic Insights into the Allosteric Modulation of Opioid Receptors by Sodium Ions #MMPMID25073009 Shang Y; LeRouzic V; Schneider S; Bisignano P; Pasternak G; Filizola M Biochemistry 2014[Aug]; 53 (31): 5140-9 PMID25073009show ga The idea of sodium ions altering G-protein-coupled receptor (GPCR) ligand binding and signaling was first suggested for opioid receptors (ORs) in the 1970s and subsequently extended to other GPCRs. Recently published ultra-high-resolution crystal structures of GPCRs, including that of the ?-OR subtype, have started to shed light on the mechanism underlying sodium control in GPCR signaling by revealing details of the sodium binding site. Whether sodium accesses different receptor subtypes from the extra- or intracellular sides, following similar or different pathways, is still an open question. Earlier experiments in brain homogenates suggested a differential sodium regulation of ligand binding to the three major OR subtypes, in spite of their high degree of sequence similarity. Intrigued by this possibility, we explored the dynamic nature of sodium binding to ?-OR, ?-OR, and ?-OR by means of microsecond-scale, all-atom molecular dynamics (MD) simulations. Rapid sodium permeation was observed exclusively from the extracellular milieu, and following similar binding pathways in all three ligand-free OR systems, notwithstanding extra densities of sodium observed near nonconserved residues of ?-OR and ?-OR, but not in ?-OR. We speculate that these differences may be responsible for the differential increase in antagonist binding affinity of ?-OR by sodium resulting from specific ligand binding experiments in transfected cells. On the other hand, sodium reduced the level of binding of subtype-specific agonists to all OR subtypes. Additional biased and unbiased MD simulations were conducted using the ?-OR ultra-high-resolution crystal structure as a model system to provide a mechanistic explanation for this experimental observation. äMechanistic Insights into the Allosteric Modulation of Opioid Receptor(epmc).pdf DeepDyve Pubget Overpricing