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10.1016/j.bbrep.2015.03.002 http://scihub22266oqcxt.onion/10.1016/j.bbrep.2015.03.002 C5668562!5668562!29124137     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29124137&cmd=llinks): Failed to open stream: HTTP request failed! 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Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation |pdf=|usr=}}{{29124137}} gab.com Text Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation JO: Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=29124137 #FOAvip C5a receptor (C5aR) is one of the major chemoattractant receptors of the druggable proteome that binds C5a, the proinflammatory polypeptide of complement cascade, triggering inflammation and SEPSIS. Here, we report the model structures of C5aR in both inactive and peptide agonist (YSFKPMPLaR; a=D-Ala) bound meta-active state. Assembled in CYANA and evolved over molecular dynamics (MD) in POPC bilayer, the inactive C5aR demonstrates a topologically unique compact heptahelical bundle topology harboring a ?-hairpin in extracellular loop 2 (ECL2), derived from the atomistic folding simulations. The peptide agonist bound meta-active C5aR deciphers the ?site2? at an atomistic resolution in the extracellular surface (ECS), in contrast to the previously hypothesized inter-helical crevice. With estimated Ki?2.75 ?M, the meta-active C5aR excellently rationalizes the IC50 (0.1?13 ?M) and EC50 (0.01?6 ?M) values, displayed by the peptide agonist in several signaling studies. Moreover, with Ki?5.3×105 ?M, the ?site2? also illustrates selectivity, by discriminating the stereochemical mutant peptide (YSFkPMPLaR; k=D-Lys), known to be inert toward C5aR, up to 1 mM concentration. Topologically juxtaposed between the structures of rhodopsin and CXCR1, the C5aR models also display excellent structural correlations with the other G-protein coupled receptors (GPCRs). The models elaborated in the current study unravel many important structural insights previously not known for regulating the agonist binding and activation mechanism of C5aR. Twit Text FOAVip Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation ????Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=29124137 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29124137 #FOAvip English Wikipedia <ref>{{Cite pmid|29124137}}</ref> Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation #MMPMID29124137 Rana S; Sahoo AR Biochem Biophys Rep 2015[May]; 1 (ä): 85-96 PMID29124137show ga C5a receptor (C5aR) is one of the major chemoattractant receptors of the druggable proteome that binds C5a, the proinflammatory polypeptide of complement cascade, triggering inflammation and SEPSIS. Here, we report the model structures of C5aR in both inactive and peptide agonist (YSFKPMPLaR; a=D-Ala) bound meta-active state. Assembled in CYANA and evolved over molecular dynamics (MD) in POPC bilayer, the inactive C5aR demonstrates a topologically unique compact heptahelical bundle topology harboring a ?-hairpin in extracellular loop 2 (ECL2), derived from the atomistic folding simulations. The peptide agonist bound meta-active C5aR deciphers the ?site2? at an atomistic resolution in the extracellular surface (ECS), in contrast to the previously hypothesized inter-helical crevice. With estimated Ki?2.75 ?M, the meta-active C5aR excellently rationalizes the IC50 (0.1?13 ?M) and EC50 (0.01?6 ?M) values, displayed by the peptide agonist in several signaling studies. Moreover, with Ki?5.3×105 ?M, the ?site2? also illustrates selectivity, by discriminating the stereochemical mutant peptide (YSFkPMPLaR; k=D-Lys), known to be inert toward C5aR, up to 1 mM concentration. Topologically juxtaposed between the structures of rhodopsin and CXCR1, the C5aR models also display excellent structural correlations with the other G-protein coupled receptors (GPCRs). The models elaborated in the current study unravel many important structural insights previously not known for regulating the agonist binding and activation mechanism of C5aR. äModel structures of inactive and peptide agonist bound C5aR: Insights (epmc).pdf DeepDyve Pubget Overpricing