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10.1021/acs.biochem.5b01195 http://scihub22266oqcxt.onion/10.1021/acs.biochem.5b01195 C5137375!5137375!26866459     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26866459&cmd=llinks): Failed to open stream: HTTP request failed! 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Structural insights into the activation of human relaxin family peptide receptor 1 by small molecule agonists |pdf=|usr=}}{{26866459}} gab.com Text Structural insights into the activation of human relaxin family peptide receptor 1 by small molecule agonists JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26866459 #FOAvip The GPCR relaxin family peptide receptor 1 (RXFP1) mediates the action of relaxin peptide hormone including its tissue remodeling and antifibrotic effects. The peptide hormone has a short half-life in plasma, limiting its therapeutic utility. However, small molecule agonists of human RXFP1 can overcome this limitation and may provide a useful therapeutic approach especially for chronic diseases such as heart failure and fibrosis. The first small molecule agonists of RXFP1 were recently identified from a high throughput screen using a homogenous cell-based cAMP assay. Optimization of the hit compounds resulted in a series of highly potent and RXFP1 selective agonists with low cytotoxicity, and excellent in vitro ADME and pharmacokinetic properties. Here we undertook extensive site-directed mutagenesis studies in combination with computational modeling analysis to probe the molecular basis of the small molecule binding to RXFP1. The results showed that the agonists bind to an allosteric site of RXFP1 in a manner that closely interacts with the seven transmembrane domain (TM7) and the third extracellular loop (ECL3). A number of residues were found to play an important role in the agonist binding and receptor activation including a hydrophobic region at TM7 consisting of W664, F668 and L670. The G659/T660 motif within ECL3 is crucial to the observed species selectivity of the agonists for RXFP1. The receptor binding and activation effects by the small molecule agonist ML290 were compared with the cognate ligand relaxin peptide, providing valuable insights on the structural basis and molecular mechanism of activation and selectivity of the agonists for RXFP1. Twit Text FOAVip Structural insights into the activation of human relaxin family peptide receptor 1 by small molecule agonists ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26866459 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26866459 #FOAvip English Wikipedia <ref>{{Cite pmid|26866459}}</ref> Structural insights into the activation of human relaxin family peptide receptor 1 by small molecule agonists #MMPMID26866459 Hu X; Myhr C; Huang Z; Xiao J; Barnaeva E; Ho BA; Agoulnik IU; Ferrer M; Marugan JJ; Southall N; Agoulnik AI Biochemistry 2016[Mar]; 55 (12): 1772-83 PMID26866459show ga The GPCR relaxin family peptide receptor 1 (RXFP1) mediates the action of relaxin peptide hormone including its tissue remodeling and antifibrotic effects. The peptide hormone has a short half-life in plasma, limiting its therapeutic utility. However, small molecule agonists of human RXFP1 can overcome this limitation and may provide a useful therapeutic approach especially for chronic diseases such as heart failure and fibrosis. The first small molecule agonists of RXFP1 were recently identified from a high throughput screen using a homogenous cell-based cAMP assay. Optimization of the hit compounds resulted in a series of highly potent and RXFP1 selective agonists with low cytotoxicity, and excellent in vitro ADME and pharmacokinetic properties. Here we undertook extensive site-directed mutagenesis studies in combination with computational modeling analysis to probe the molecular basis of the small molecule binding to RXFP1. The results showed that the agonists bind to an allosteric site of RXFP1 in a manner that closely interacts with the seven transmembrane domain (TM7) and the third extracellular loop (ECL3). A number of residues were found to play an important role in the agonist binding and receptor activation including a hydrophobic region at TM7 consisting of W664, F668 and L670. The G659/T660 motif within ECL3 is crucial to the observed species selectivity of the agonists for RXFP1. The receptor binding and activation effects by the small molecule agonist ML290 were compared with the cognate ligand relaxin peptide, providing valuable insights on the structural basis and molecular mechanism of activation and selectivity of the agonists for RXFP1. äStructural insights into the activation of human relaxin family peptid(epmc).pdf DeepDyve Pubget Overpricing