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10.1073/pnas.1719834115 http://scihub22266oqcxt.onion/10.1073/pnas.1719834115 C5798384!5798384 !29343645     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29343645 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29343645 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (5 ): E896-E905 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 a potent bacterial endotoxin that triggers the innate immune system. Proper recognition of LPS by pattern-recognition receptors requires a full complement of typically six acyl chains in the lipid portion. Acyloxyacyl hydrolase (AOAH) is a host enzyme that removes secondary (acyloxyacyl-linked) fatty acids from LPS, rendering it immunologically inert. This activity is critical for recovery from immune tolerance that follows Gram-negative infection. To understand the molecular mechanism of AOAH function, we determined its crystal structure and its complex with LPS. The substrate's lipid moiety is accommodated in a large hydrophobic pocket formed by the saposin and catalytic domains with a secondary acyl chain inserted into a narrow lateral hydrophobic tunnel at the active site. The enzyme establishes dispensable contacts with the phosphate groups of LPS but does not interact with its oligosaccharide portion. Proteolytic processing allows movement of an amphipathic helix possibly involved in substrate access at membranes. 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-E905 PMID29343645 show ga LPS is a potent bacterial endotoxin that triggers the innate immune system. Proper recognition of LPS by pattern-recognition receptors requires a full complement of typically six acyl chains in the lipid portion. Acyloxyacyl hydrolase (AOAH) is a host enzyme that removes secondary (acyloxyacyl-linked) fatty acids from LPS, rendering it immunologically inert. This activity is critical for recovery from immune tolerance that follows Gram-negative infection. To understand the molecular mechanism of AOAH function, we determined its crystal structure and its complex with LPS. The substrate's lipid moiety is accommodated in a large hydrophobic pocket formed by the saposin and catalytic domains with a secondary acyl chain inserted into a narrow lateral hydrophobic tunnel at the active site. The enzyme establishes dispensable contacts with the phosphate groups of LPS but does not interact with its oligosaccharide portion. Proteolytic processing allows movement of an amphipathic helix possibly involved in substrate access at membranes. |Animals [MESH] |Calcium/chemistry [MESH] |Carboxylic Ester Hydrolases/*chemistry [MESH] |Catalytic Domain [MESH] |Cell Membrane/metabolism [MESH] |Crystallography, X-Ray [MESH] |Endosomes/metabolism [MESH] |Humans [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Immune System [MESH] |Lipopolysaccharides/*chemistry [MESH] |Mice [MESH] |Protein Binding [MESH] |Protein Domains [MESH] |Protein Structure, Secondary [MESH] |Rabbits [MESH] |Saposins/chemistry [MESH] |Scattering, Radiation [MESH] |Surface Properties [MESH]Crystal structure of the mammalian lipopolysaccharide detoxifier (epmc).pdf DeepDyve Pubget Overpricing