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TitleStructural basis of soluble membrane attack complex packaging for clearance.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 6086, Year 2021
Publish dateOct 19, 2021
AuthorsAnaïs Menny / Marie V Lukassen / Emma C Couves / Vojtech Franc / Albert J R Heck / Doryen Bubeck /
PubMed AbstractUnregulated complement activation causes inflammatory and immunological pathologies with consequences for human disease. To prevent bystander damage during an immune response, extracellular ...Unregulated complement activation causes inflammatory and immunological pathologies with consequences for human disease. To prevent bystander damage during an immune response, extracellular chaperones (clusterin and vitronectin) capture and clear soluble precursors to the membrane attack complex (sMAC). However, how these chaperones block further polymerization of MAC and prevent the complex from binding target membranes remains unclear. Here, we address that question by combining cryo electron microscopy (cryoEM) and cross-linking mass spectrometry (XL-MS) to solve the structure of sMAC. Together our data reveal how clusterin recognizes and inhibits polymerizing complement proteins by binding a negatively charged surface of sMAC. Furthermore, we show that the pore-forming C9 protein is trapped in an intermediate conformation whereby only one of its two transmembrane β-hairpins has unfurled. This structure provides molecular details for immune pore formation and helps explain a complement control mechanism that has potential implications for how cell clearance pathways mediate immune homeostasis.
External linksNat Commun / PubMed:34667172 / PubMed Central
MethodsEM (single particle)
Resolution3.27 - 3.83 Å
Structure data

EMDB-12646:
cryoEM reconstruction of the terminal C9s and chaperone in 3C9-sMAC
Method: EM (single particle) / Resolution: 3.83 Å

EMDB-12647:
cryoEM reconstruction of the terminal C9s in 2C9-sMAC
Method: EM (single particle) / Resolution: 3.34 Å

EMDB-12648:
cryoEM reconstruction of C5b and C7 C-ter in 2C9-sMAC
Method: EM (single particle) / Resolution: 3.64 Å

EMDB-12649:
cryoEM reconstruction of 1C9-sMAC
Method: EM (single particle) / Resolution: 3.8 Å

12650

7nyc

EMDB-12650, PDB-7nyc:
cryoEM structure of 3C9-sMAC
Method: EM (single particle) / Resolution: 3.54 Å

12651

7nyd

EMDB-12651, PDB-7nyd:
cryoEM structure of 2C9-sMAC
Method: EM (single particle) / Resolution: 3.27 Å

Chemicals

ChemComp-BMA:
beta-D-mannopyranose / Mannose

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-FUC:
alpha-L-fucopyranose / Fucose

Source
  • homo sapiens (human)
  • Human (human)
KeywordsIMMUNE SYSTEM / Complement / MACPF / Membrane Attack Complex / CDC / pore forming

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