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10.1074/jbc.M117.776476 http://scihub22266oqcxt.onion/10.1074/jbc.M117.776476 C5473249!5473249!28438838     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2017 ; 292 (24): 9975-87 Nephropedia Template TP {{tp|p=28438838|t=2017. Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab |pdf=|usr=}}{{28438838}} gab.com Text Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28438838 #FOAvip Immunoglobulin E and its interactions with receptors Fc?RI and CD23 play a central role in allergic disease. Omalizumab, a clinically approved therapeutic antibody, inhibits the interaction between IgE and Fc?RI, preventing mast cell and basophil activation, and blocks IgE binding to CD23 on B cells and antigen-presenting cells. We solved the crystal structure of the complex between an omalizumab-derived Fab and IgE-Fc, with one Fab bound to each C?3 domain. Free IgE-Fc adopts an acutely bent structure, but in the complex it is only partially bent, with large-scale conformational changes in the C?3 domains that inhibit the interaction with Fc?RI. CD23 binding is inhibited sterically due to overlapping binding sites on each C?3 domain. Studies of omalizumab Fab binding in solution demonstrate the allosteric basis for Fc?RI inhibition and, together with the structure, reveal how omalizumab may accelerate dissociation of receptor-bound IgE from Fc?RI, exploiting the intrinsic flexibility and allosteric potential of IgE. Twit Text FOAVip Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28438838 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28438838 #FOAvip English Wikipedia <ref>{{Cite pmid|28438838}}</ref> Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab #MMPMID28438838 Davies AM; Allan EG; Keeble AH; Delgado J; Cossins BP; Mitropoulou AN; Pang MOY; Ceska T; Beavil AJ; Craggs G; Westwood M; Henry AJ; McDonnell JM; Sutton BJ J Biol Chem 2017[Jun]; 292 (24): 9975-87 PMID28438838show ga Immunoglobulin E and its interactions with receptors Fc?RI and CD23 play a central role in allergic disease. Omalizumab, a clinically approved therapeutic antibody, inhibits the interaction between IgE and Fc?RI, preventing mast cell and basophil activation, and blocks IgE binding to CD23 on B cells and antigen-presenting cells. We solved the crystal structure of the complex between an omalizumab-derived Fab and IgE-Fc, with one Fab bound to each C?3 domain. Free IgE-Fc adopts an acutely bent structure, but in the complex it is only partially bent, with large-scale conformational changes in the C?3 domains that inhibit the interaction with Fc?RI. CD23 binding is inhibited sterically due to overlapping binding sites on each C?3 domain. Studies of omalizumab Fab binding in solution demonstrate the allosteric basis for Fc?RI inhibition and, together with the structure, reveal how omalizumab may accelerate dissociation of receptor-bound IgE from Fc?RI, exploiting the intrinsic flexibility and allosteric potential of IgE. äAllosteric mechanism of action of the therapeutic anti-IgE antibody om(epmc).pdf DeepDyve Pubget Overpricing