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10.1073/pnas.1707856115 http://scihub22266oqcxt.onion/10.1073/pnas.1707856115 C5776790!5776790 !29247053     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29247053 &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       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (1 ): E72-E81 Nephropedia Template TP {{tp|p=29247053 |t=2018. Affimer proteins inhibit immune complex binding to Fc?RIIIa with high specificity through competitive and allosteric modes of action |pdf=|usr=}}{{29247053 }} gab.com Text Affimer proteins inhibit immune complex binding to Fc RIIIa with high specificity through competitive and allosteric modes of action JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29247053 #FOAvip Protein-protein interactions are essential for the control of cellular functions and are critical for regulation of the immune system. One example is the binding of Fc regions of IgG to the Fc gamma receptors (Fc?Rs). High sequence identity (98%) between the genes encoding Fc?RIIIa (expressed on macrophages and natural killer cells) and Fc?RIIIb (expressed on neutrophils) has prevented the development of monospecific agents against these therapeutic targets. We now report the identification of Fc?RIIIa-specific artificial binding proteins called "Affimer" that block IgG binding and abrogate Fc?RIIIa-mediated downstream effector functions in macrophages, namely TNF release and phagocytosis. Cocrystal structures and molecular dynamics simulations have revealed the structural basis of this specificity for two Affimer proteins: One binds directly to the Fc binding site, whereas the other acts allosterically. Twit Text FOAVip Affimer proteins inhibit immune complex binding to Fc RIIIa with high specificity through competitive and allosteric modes of action ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29247053 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29247053 #FOAvip English Wikipedia <ref>{{Cite pmid|29247053 }}</ref> Affimer proteins inhibit immune complex binding to Fc?RIIIa with high specificity through competitive and allosteric modes of action #MMPMID29247053 Robinson JI ; Baxter EW ; Owen RL ; Thomsen M ; Tomlinson DC ; Waterhouse MP ; Win SJ ; Nettleship JE ; Tiede C ; Foster RJ ; Owens RJ ; Fishwick CWG ; Harris SA ; Goldman A ; McPherson MJ ; Morgan AW Proc Natl Acad Sci U S A 2018[Jan]; 115 (1 ): E72-E81 PMID29247053 show ga Protein-protein interactions are essential for the control of cellular functions and are critical for regulation of the immune system. One example is the binding of Fc regions of IgG to the Fc gamma receptors (Fc?Rs). High sequence identity (98%) between the genes encoding Fc?RIIIa (expressed on macrophages and natural killer cells) and Fc?RIIIb (expressed on neutrophils) has prevented the development of monospecific agents against these therapeutic targets. We now report the identification of Fc?RIIIa-specific artificial binding proteins called "Affimer" that block IgG binding and abrogate Fc?RIIIa-mediated downstream effector functions in macrophages, namely TNF release and phagocytosis. Cocrystal structures and molecular dynamics simulations have revealed the structural basis of this specificity for two Affimer proteins: One binds directly to the Fc binding site, whereas the other acts allosterically. |*Molecular Dynamics Simulation [MESH] |Allosteric Regulation [MESH] |Antigen-Antibody Complex/*chemistry/immunology [MESH] |Humans [MESH] |Immunoglobulin G/*chemistry/immunology [MESH]Affimer proteins inhibit immune complex binding to Fc?RIIIa with high (epmc).pdf DeepDyve Pubget Overpricing