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10.15252/embj.201696173 http://scihub22266oqcxt.onion/10.15252/embj.201696173 C5391138!5391138!28264884     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 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\28264884.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       EMBO+J 2017 ; 36 (8): 1084-99 Nephropedia Template TP {{tp|p=28264884|t=2017. Functional and structural insight into properdin control of complement alternative pathway amplification |pdf=|usr=}}{{28264884}} gab.com Text Functional and structural insight into properdin control of complement alternative pathway amplification JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=28264884 #FOAvip Properdin (FP) is an essential positive regulator of the complement alternative pathway (AP) providing stabilization of the C3 and C5 convertases, but its oligomeric nature challenges structural analysis. We describe here a novel FP deficiency (E244K) caused by a single point mutation which results in a very low level of AP activity. Recombinant FP E244K is monomeric, fails to support bacteriolysis, and binds weakly to C3 products. We compare this to a monomeric unit excised from oligomeric FP, which is also dysfunctional in bacteriolysis but binds the AP proconvertase, C3 convertase, C3 products and partially stabilizes the convertase. The crystal structure of such a FP?convertase complex suggests that the major contact between FP and the AP convertase is mediated by a single FP thrombospondin repeat and a small region in C3b. Small angle X?ray scattering indicates that FP E244K is trapped in a compact conformation preventing its oligomerization. Our studies demonstrate an essential role of FP oligomerization in vivo while our monomers enable detailed structural insight paving the way for novel modulators of complement. Twit Text FOAVip Functional and structural insight into properdin control of complement alternative pathway amplification ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=28264884 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28264884 #FOAvip English Wikipedia <ref>{{Cite pmid|28264884}}</ref> Functional and structural insight into properdin control of complement alternative pathway amplification #MMPMID28264884 Pedersen DV; Roumenina L; Jensen RK; Gadeberg TA; Marinozzi C; Picard C; Rybkine T; Thiel S; Sørensen UB; Stover C; Fremeaux?Bacchi V; Andersen GR EMBO J 2017[Apr]; 36 (8): 1084-99 PMID28264884show ga Properdin (FP) is an essential positive regulator of the complement alternative pathway (AP) providing stabilization of the C3 and C5 convertases, but its oligomeric nature challenges structural analysis. We describe here a novel FP deficiency (E244K) caused by a single point mutation which results in a very low level of AP activity. Recombinant FP E244K is monomeric, fails to support bacteriolysis, and binds weakly to C3 products. We compare this to a monomeric unit excised from oligomeric FP, which is also dysfunctional in bacteriolysis but binds the AP proconvertase, C3 convertase, C3 products and partially stabilizes the convertase. The crystal structure of such a FP?convertase complex suggests that the major contact between FP and the AP convertase is mediated by a single FP thrombospondin repeat and a small region in C3b. Small angle X?ray scattering indicates that FP E244K is trapped in a compact conformation preventing its oligomerization. Our studies demonstrate an essential role of FP oligomerization in vivo while our monomers enable detailed structural insight paving the way for novel modulators of complement. äFunctional and structural insight into properdin control of complement(epmc).pdf DeepDyve Pubget Overpricing