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TitleStructural basis of complement membrane attack complex formation.
Journal, issue, pagesNat Commun, Vol. 7, Page 10587, Year 2016
Publish dateFeb 4, 2016
AuthorsMarina Serna / Joanna L Giles / B Paul Morgan / Doryen Bubeck /
PubMed AbstractIn response to complement activation, the membrane attack complex (MAC) assembles from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses pathogens by a 'multi-hit' mechanism; ...In response to complement activation, the membrane attack complex (MAC) assembles from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses pathogens by a 'multi-hit' mechanism; however, sublytic MAC pores on host cells activate signalling pathways. Previous studies have described the structures of individual MAC components and subcomplexes; however, the molecular details of its assembly and mechanism of action remain unresolved. Here we report the electron cryo-microscopy structure of human MAC at subnanometre resolution. Structural analyses define the stoichiometry of the complete pore and identify a network of interaction interfaces that determine its assembly mechanism. MAC adopts a 'split-washer' configuration, in contrast to the predicted closed ring observed for perforin and cholesterol-dependent cytolysins. Assembly precursors partially penetrate the lipid bilayer, resulting in an irregular β-barrel pore. Our results demonstrate how differences in symmetric and asymmetric components of the MAC underpin a molecular basis for pore formation and suggest a mechanism of action that extends beyond membrane penetration.
External linksNat Commun / PubMed:26841837 / PubMed Central
MethodsEM (single particle)
Resolution7.3 - 8.5 Å
Structure data

EMDB-3134:
Electron cryo-microscopy of an immune pore
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-3135:
Electron cryo-microscopy of an immune pore
Method: EM (single particle) / Resolution: 7.3 Å

Source
  • Homo sapiens (human)

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