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TitleStructural basis for the stabilization of the complement alternative pathway C3 convertase by properdin.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 33, Page 13504-13509, Year 2013
Publish dateAug 13, 2013
AuthorsMartín Alcorlo / Agustín Tortajada / Santiago Rodríguez de Córdoba / Oscar Llorca /
PubMed AbstractComplement is an essential component of innate immunity. Its activation results in the assembly of unstable protease complexes, denominated C3/C5 convertases, leading to inflammation and lysis. ...Complement is an essential component of innate immunity. Its activation results in the assembly of unstable protease complexes, denominated C3/C5 convertases, leading to inflammation and lysis. Regulatory proteins inactivate C3/C5 convertases on host surfaces to avoid collateral tissue damage. On pathogen surfaces, properdin stabilizes C3/C5 convertases to efficiently fight infection. How properdin performs this function is, however, unclear. Using electron microscopy we show that the N- and C-terminal ends of adjacent monomers in properdin oligomers conform a curly vertex that holds together the AP convertase, interacting with both the C345C and vWA domains of C3b and Bb, respectively. Properdin also promotes a large displacement of the TED (thioester-containing domain) and CUB (complement protein subcomponents C1r/C1s, urchin embryonic growth factor and bone morphogenetic protein 1) domains of C3b, which likely impairs C3-convertase inactivation by regulatory proteins. The combined effect of molecular cross-linking and structural reorganization increases stability of the C3 convertase and facilitates recruitment of fluid-phase C3 convertase to the cell surfaces. Our model explains how properdin mediates the assembly of stabilized C3/C5-convertase clusters, which helps to localize complement amplification to pathogen surfaces.
External linksProc Natl Acad Sci U S A / PubMed:23901101 / PubMed Central
MethodsEM (single particle)
Resolution23.4 - 29.3 Å
Structure data

EMDB-2402:
3D structure of a properdin vertex
Method: EM (single particle) / Resolution: 23.4 Å

EMDB-2403:
Structure of Human C3bBb convertase bound to a fragment of Properdin
Method: EM (single particle) / Resolution: 29.3 Å

Source
  • Homo sapiens (human)

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