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Literature summary for 3.4.21.47 extracted from

  • Torreira, E.; Tortajada, A.; Montes, T.; Rodriguez de Cordoba, S.; Llorca, O.
    3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase (2009), Proc. Natl. Acad. Sci. USA, 106, 882-887.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
factor B generation of the AP C3-convertase initiates by the binding of factor B to C3b to form the proconvertase, C3bB. Factor B undergoes a dramatic conformational change upon binding to C3b, it binds near the C345C domain in C3b. Factor B-D279G mutant promotes high-affinity C3b-binding and is correctly cleaved by factor D in the C3bB proenzyme to generate a very stable, functionally-active, AP C3-convertase C3bBb Homo sapiens
factor D the proconvertase C3bB is cleaved by factor D at a single site in factor B, producing Ba and Bb fragments. Ba dissociates from the complex, while Bb remains bound to C3b, forming the active AP C3-convertase C3bBb Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
complement receptor 1 CR1, mediates decay acceleration of the C3bBb complex Homo sapiens
decay accelerating factor DAF, mediates decay acceleration of the C3bBb complex Homo sapiens
factor H mediates decay acceleration of the C3bBb complex Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ promotes a stable C3bB complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00751
-
-

Purification (Commentary)

Purification (Comment) Organism
C3bB(Ni2+) complex or C3bBb(factor B-D279G mutant) purified by gel filtration Homo sapiens

Synonyms

Synonyms Comment Organism
alternative pathway C3-convertase
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Homo sapiens
AP C3-convertase
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Homo sapiens
C3bB complex
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Homo sapiens