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10.1038/ncomms9013 http://scihub22266oqcxt.onion/10.1038/ncomms9013 C4547401!4547401!26289479     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2015 ; 6 (ä): ä Nephropedia Template TP {{tp|p=26289479|t=2015. Structural mechanism for signal transduction in RXR nuclear receptor heterodimers |pdf=|usr=}}{{26289479}} gab.com Text Structural mechanism for signal transduction in RXR nuclear receptor heterodimers JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26289479 #FOAvip A subset of nuclear receptors (NRs) function as obligate heterodimers with retinoid X receptor (RXR), allowing integration of ligand-dependent signals across the dimer interface via an unknown structural mechanism. Using nuclear magnetic resonance (NMR) spectroscopy, x-ray crystallography and hydrogen/deuterium exchange (HDX) mass spectrometry, here we show an allosteric mechanism through which RXR co-operates with a permissive dimer partner, peroxisome proliferator-activated receptor (PPAR)-?, while rendered generally unresponsive by a non-permissive dimer partner, thyroid hormone (TR) receptor. Amino acid residues that mediate this allosteric mechanism comprise an evolutionarily conserved network discovered by statistical coupling analysis (SCA). This SCA network acts as a signalling rheostat to integrate signals between dimer partners, ligands and coregulator-binding sites, thereby affecting signal transmission in RXR heterodimers. These findings define rules guiding how NRs integrate two ligand-dependent signalling pathways into RXR heterodimer-specific responses. Twit Text FOAVip Structural mechanism for signal transduction in RXR nuclear receptor heterodimers ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26289479 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26289479 #FOAvip English Wikipedia <ref>{{Cite pmid|26289479}}</ref> Structural mechanism for signal transduction in RXR nuclear receptor heterodimers #MMPMID26289479 Kojetin DJ; Matta-Camacho E; Hughes TS; Srinivasan S; Nwachukwu JC; Cavett V; Nowak J; Chalmers MJ; Marciano DP; Kamenecka TM; Shulman AI; Rance M; Griffin PR; Bruning JB; Nettles KW Nat Commun 2015[]; 6 (ä): ä PMID26289479show ga A subset of nuclear receptors (NRs) function as obligate heterodimers with retinoid X receptor (RXR), allowing integration of ligand-dependent signals across the dimer interface via an unknown structural mechanism. Using nuclear magnetic resonance (NMR) spectroscopy, x-ray crystallography and hydrogen/deuterium exchange (HDX) mass spectrometry, here we show an allosteric mechanism through which RXR co-operates with a permissive dimer partner, peroxisome proliferator-activated receptor (PPAR)-?, while rendered generally unresponsive by a non-permissive dimer partner, thyroid hormone (TR) receptor. Amino acid residues that mediate this allosteric mechanism comprise an evolutionarily conserved network discovered by statistical coupling analysis (SCA). This SCA network acts as a signalling rheostat to integrate signals between dimer partners, ligands and coregulator-binding sites, thereby affecting signal transmission in RXR heterodimers. These findings define rules guiding how NRs integrate two ligand-dependent signalling pathways into RXR heterodimer-specific responses. äStructural mechanism for signal transduction in RXR nuclear receptor h(epmc).pdf DeepDyve Pubget Overpricing