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10.1073/pnas.1719834115 http://scihub22266oqcxt.onion/10.1073/pnas.1719834115 C5798384!5798384!29343645     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       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (5): E896-905 Nephropedia Template TP {{tp|p=29343645|t=2018. Crystal structure of the mammalian lipopolysaccharide detoxifier |pdf=|usr=}}{{29343645}} gab.com Text Crystal structure of the mammalian lipopolysaccharide detoxifier JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29343645 #FOAvip LPS is the major bacterial molecule recognized by the human innate immune system. It elicits a strong inflammatory response followed by a state of immune tolerance. The human enzyme acyloxyacyl hydrolase (AOAH) then detoxifies LPS to reestablish sensitivity for subsequent infections. We determined the 3D structure of AOAH to better understand its function. The enzyme binds to LPS via a hydrophobic surface and contains a hydrophobic tunnel into which one fatty acyl chain of the LPS fits to be cleaved off. AOAH also interacts with the phosphate groups of LPS but not its saccharide portion. Additionally, we report an unexpected calcium-binding domain in this enzyme. Twit Text FOAVip Crystal structure of the mammalian lipopolysaccharide detoxifier ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29343645 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29343645 #FOAvip English Wikipedia <ref>{{Cite pmid|29343645}}</ref> Crystal structure of the mammalian lipopolysaccharide detoxifier #MMPMID29343645 Gorelik A; Illes K; Nagar B Proc Natl Acad Sci U S A 2018[Jan]; 115 (5): E896-905 PMID29343645show ga LPS is the major bacterial molecule recognized by the human innate immune system. It elicits a strong inflammatory response followed by a state of immune tolerance. The human enzyme acyloxyacyl hydrolase (AOAH) then detoxifies LPS to reestablish sensitivity for subsequent infections. We determined the 3D structure of AOAH to better understand its function. The enzyme binds to LPS via a hydrophobic surface and contains a hydrophobic tunnel into which one fatty acyl chain of the LPS fits to be cleaved off. AOAH also interacts with the phosphate groups of LPS but not its saccharide portion. Additionally, we report an unexpected calcium-binding domain in this enzyme. äCrystal structure of the mammalian lipopolysaccharide detoxifier (epmc).pdf DeepDyve Pubget Overpricing