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10.1074/jbc.M115.639021 http://scihub22266oqcxt.onion/10.1074/jbc.M115.639021 C4432280!4432280 !25795782     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25795782 &cmd=llinks): Failed to open stream: HTTP request failed! 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Systemic lupus erythematosus-associated neutrophil cytosolic factor 2 mutation affects the structure of NADPH oxidase complex |pdf=|usr=}}{{25795782 }} gab.com Text Systemic lupus erythematosus-associated neutrophil cytosolic factor 2 mutation affects the structure of NADPH oxidase complex JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25795782 #FOAvip In a case-control association study with 3716 North Americans of Hispanic descent and 4867 North Americans of European descent, we show that the associations of rs17849502 (NCF2 His-389 ? Gln) and rs13306575 (NCF2 Arg-395 ? Trp) with systemic lupus erythematosus are independent. We have shown that His-389 ? Gln disrupts the binding of NCF2 to the ZF domain of VAV1, resulting in decreased NADPH oxidase activity. With respect to Arg-395 ? Trp, using protein docking and structure analyses, we provide a model for the involvement of this mutation in the structure and function of the NADPH oxidase complex. This model assigns a central role to Arg-395 in the structure and stability of the quaternary NCF2/NCF4/VAV1/RAC1 NADPH oxidase complex. Arg-395 stabilizes the C-terminal tail of NCF4 and the conformation of NCF2 loop 395-402, which in turn stabilize the evolutionarily conserved interactions of NCF2/NCF4 with the DH domain of VAV1 and RAC1 region 120-137. Our findings are consistent with the high levels of conservation of all of the residues involved in these interactions. Twit Text FOAVip Systemic lupus erythematosus-associated neutrophil cytosolic factor 2 mutation affects the structure of NADPH oxidase complex ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25795782 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25795782 #FOAvip English Wikipedia <ref>{{Cite pmid|25795782 }}</ref> Systemic lupus erythematosus-associated neutrophil cytosolic factor 2 mutation affects the structure of NADPH oxidase complex #MMPMID25795782 Armstrong DL ; Eisenstein M ; Zidovetzki R ; Jacob CO J Biol Chem 2015[May]; 290 (20 ): 12595-602 PMID25795782 show ga In a case-control association study with 3716 North Americans of Hispanic descent and 4867 North Americans of European descent, we show that the associations of rs17849502 (NCF2 His-389 ? Gln) and rs13306575 (NCF2 Arg-395 ? Trp) with systemic lupus erythematosus are independent. We have shown that His-389 ? Gln disrupts the binding of NCF2 to the ZF domain of VAV1, resulting in decreased NADPH oxidase activity. With respect to Arg-395 ? Trp, using protein docking and structure analyses, we provide a model for the involvement of this mutation in the structure and function of the NADPH oxidase complex. This model assigns a central role to Arg-395 in the structure and stability of the quaternary NCF2/NCF4/VAV1/RAC1 NADPH oxidase complex. Arg-395 stabilizes the C-terminal tail of NCF4 and the conformation of NCF2 loop 395-402, which in turn stabilize the evolutionarily conserved interactions of NCF2/NCF4 with the DH domain of VAV1 and RAC1 region 120-137. Our findings are consistent with the high levels of conservation of all of the residues involved in these interactions. |*Lupus Erythematosus, Systemic [MESH] |*Molecular Docking Simulation [MESH] |*Mutation, Missense [MESH] |Amino Acid Substitution [MESH] |Enzyme Stability/genetics [MESH] |Female [MESH] |Hispanic or Latino [MESH] |Humans [MESH] |Male [MESH] |NADPH Oxidases/*chemistry/genetics/metabolism [MESH] |Phosphoproteins/chemistry/genetics/metabolism [MESH] |Protein Structure, Quaternary [MESH] |Protein Structure, Tertiary [MESH] |Proto-Oncogene Proteins c-vav/chemistry/genetics/metabolism [MESH] |White People [MESH]Systemic lupus erythematosus-associated neutrophil cytosolic factor 2 (epmc).pdf DeepDyve Pubget Overpricing