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Literature summary for 3.4.21.47 extracted from

  • Alcorlo, M.; Tortajada, A.; Rodriguez de Cordoba, S.; Llorca, O.
    Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin (2013), Proc. Natl. Acad. Sci. USA, 110, 13504-13509.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
additional information regulatory proteins inactivate C3/C5 convertases on host surfaces to avoid collateral tissue damage Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P00751
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
C3 convertase
-
 Homo sapiens
complement alternative pathway C3 convertase
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism complement 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, the glycoprotein properdin stabilizes C3/C5 convertases to efficiently fight infection. 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 (thioestercontaining 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 Homo sapiens
additional information stabilization of the complement alternative pathway C3 convertase by properdin, structural basis, overview. Complex assembly between properdin and C3 convertase by incubation of C3b, Factor B, and Factor D in the presence of properdin. The Factor B-D279G mutant increases the stability of C3 convertase. Properdin cross-Links C3b and the Bb fragment, stabilizing the C3bBb convertase, structure overview Homo sapiens