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Structure of the poly-C9 component of the complement membrane attack complex.
Dudkina, Natalya V; Spicer, Bradley A; Reboul, Cyril F; Conroy, Paul J; Lukoyanova, Natalya; Elmlund, Hans; Law, Ruby H P; Ekkel, Susan M; Kondos, Stephanie C; Goode, Robert J A; Ramm, Georg; Whisstock, James C; Saibil, Helen R; Dunstone, Michelle A.
Afiliação
  • Dudkina NV; Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
  • Spicer BA; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Reboul CF; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Conroy PJ; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Lukoyanova N; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Elmlund H; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Law RH; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Ekkel SM; Department of Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
  • Kondos SC; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Goode RJ; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Ramm G; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Whisstock JC; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Saibil HR; ARC Centre of Excellence in Advanced Molecular Imaging, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
  • Dunstone MA; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Clayton Campus, Monash University, Melbourne, Victoria 3800, Australia.
Nat Commun ; 7: 10588, 2016 Feb 04.
Article em En | MEDLINE | ID: mdl-26841934
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 ß-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.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polímeros / Complemento C9 / Complexo de Ataque à Membrana do Sistema Complemento Limite: Humans Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Polímeros / Complemento C9 / Complexo de Ataque à Membrana do Sistema Complemento Limite: Humans Idioma: En Revista: Nat Commun Assunto da revista: BIOLOGIA / CIENCIA Ano de publicação: 2016 Tipo de documento: Article