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5FMW

The poly-C9 component of the Complement Membrane Attack Complex

5FMW の概要
エントリーDOI10.2210/pdb5fmw/pdb
EMDBエントリー3235
分子名称POLYC9 (1 entity in total)
機能のキーワードstructural protein, pore-forming protein, complement, c9, macpf
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Secreted : P02748
タンパク質・核酸の鎖数22
化学式量合計1266823.16
構造登録者
主引用文献Dudkina, N.V.,Spicer, B.A.,Reboul, C.F.,Conroy, P.J.,Lukoyanova, N.,Elmlund, H.,Law, R.H.P.,Ekkel, S.M.,Kondos, S.C.,Goode, R.J.A.,Ramm, G.,Whisstock, J.C.,Saibil, H.R.,Dunstone, M.A.
Structure of the Poly-C9 Component of the Complement Membrane Attack Complex
Nat.Commun., 7:10588-, 2016
Cited by
PubMed Abstract: 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 β-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.
PubMed: 26841934
DOI: 10.1038/NCOMMS10588
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (6.7 Å)
構造検証レポート
Validation report summary of 5fmw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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