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TitleStructures of C1-IgG1 provide insights into how danger pattern recognition activates complement.
Journal, issue, pagesScience, Vol. 359, Issue 6377, Page 794-797, Year 2018
Publish dateFeb 16, 2018
AuthorsDeniz Ugurlar / Stuart C Howes / Bart-Jan de Kreuk / Roman I Koning / Rob N de Jong / Frank J Beurskens / Janine Schuurman / Abraham J Koster / Thomas H Sharp / Paul W H I Parren / Piet Gros /
PubMed AbstractDanger patterns on microbes or damaged host cells bind and activate C1, inducing innate immune responses and clearance through the complement cascade. How these patterns trigger complement initiation ...Danger patterns on microbes or damaged host cells bind and activate C1, inducing innate immune responses and clearance through the complement cascade. How these patterns trigger complement initiation remains elusive. Here, we present cryo-electron microscopy analyses of C1 bound to monoclonal antibodies in which we observed heterogeneous structures of single and clustered C1-immunoglobulin G1 (IgG1) hexamer complexes. Distinct C1q binding sites are observed on the two Fc-CH2 domains of each IgG molecule. These are consistent with known interactions and also reveal additional interactions, which are supported by functional IgG1-mutant analysis. Upon antibody binding, the C1q arms condense, inducing rearrangements of the C1rs proteases and tilting C1q's cone-shaped stalk. The data suggest that C1r may activate C1s within single, strained C1 complexes or between neighboring C1 complexes on surfaces.
External linksScience / PubMed:29449492
MethodsEM (subtomogram averaging) / EM (single particle)
Resolution10.0 - 25.0 Å
Structure data

EMDB-4231:
C1-IgG1 complex on liposomes
Method: EM (subtomogram averaging) / Resolution: 25.0 Å

4232

6fcz

EMDB-4232: Cryo-EM reconstruction of C1-IgG1 complex
PDB-6fcz: Model of gC1q-Fc complex based on 7A EM map
Method: EM (single particle) / Resolution: 10.0 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • Human (human)
KeywordsIMMUNE SYSTEM / Complement / antibody / complex / C1

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