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10.1038/ncomms10588 http://scihub22266oqcxt.onion/10.1038/ncomms10588 C4742998!4742998!26841934     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2016 ; 7 (ä): ä Nephropedia Template TP {{tp|p=26841934|t=2016. Structure of the poly-C9 component of the complement membrane attack complex |pdf=|usr=}}{{26841934}} gab.com Text Structure of the poly-C9 component of the complement membrane attack complex JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26841934 #FOAvip The membrane attack complex (MAC)/perforin-like protein complement component 9 (C9) is the major component of the MAC, a multi-protein complex that forms pores in the membrane of target pathogens. In contrast to homologous proteins such as perforin and the cholesterol-dependent cytolysins (CDCs), all of which require the membrane for oligomerisation, C9 assembles directly onto the nascent MAC from solution. However, the molecular mechanism of MAC assembly remains to be understood. Here we present the 8?Å cryo-EM structure of a soluble form of the poly-C9 component of the MAC. These data reveal a 22-fold symmetrical arrangement of C9 molecules that yield an 88-strand pore-forming ?-barrel. The N-terminal thrombospondin-1 (TSP1) domain forms an unexpectedly extensive part of the oligomerisation interface, thus likely facilitating solution-based assembly. These TSP1 interactions may also explain how additional C9 subunits can be recruited to the growing MAC subsequent to membrane insertion. Twit Text FOAVip Structure of the poly-C9 component of the complement membrane attack complex ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26841934 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26841934 #FOAvip English Wikipedia <ref>{{Cite pmid|26841934}}</ref> Structure of the poly-C9 component of the complement membrane attack complex #MMPMID26841934 Dudkina NV; Spicer BA; Reboul CF; Conroy PJ; Lukoyanova N; Elmlund H; Law RHP; Ekkel SM; Kondos SC; Goode RJA; Ramm G; Whisstock JC; Saibil HR; Dunstone MA Nat Commun 2016[]; 7 (ä): ä PMID26841934show ga The membrane attack complex (MAC)/perforin-like protein complement component 9 (C9) is the major component of the MAC, a multi-protein complex that forms pores in the membrane of target pathogens. In contrast to homologous proteins such as perforin and the cholesterol-dependent cytolysins (CDCs), all of which require the membrane for oligomerisation, C9 assembles directly onto the nascent MAC from solution. However, the molecular mechanism of MAC assembly remains to be understood. Here we present the 8?Å cryo-EM structure of a soluble form of the poly-C9 component of the MAC. These data reveal a 22-fold symmetrical arrangement of C9 molecules that yield an 88-strand pore-forming ?-barrel. The N-terminal thrombospondin-1 (TSP1) domain forms an unexpectedly extensive part of the oligomerisation interface, thus likely facilitating solution-based assembly. These TSP1 interactions may also explain how additional C9 subunits can be recruited to the growing MAC subsequent to membrane insertion. äStructure of the poly-C9 component of the complement membrane attack c(epmc).pdf DeepDyve Pubget Overpricing