Complement C3

spinqualitylabelsall models Structure of human glycosylated complement C3bα (magenta) and β (salmon) chains complex with protein CRIG (cyan) and Ca+2 ion (green) (PDB code 2icf). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Complement C3 (CC3) activates the complement system which is part of the immune response. CC3 is proteolytically cleaved by C3 convertase to C3a (residues 672-748) and C3b (residues 23-667, 749-1663). C3a is a mediator of local inflammatory processes. C3b binds covalently to cell surface carbohydrates or immune aggregates. Breakdown of C3b generates the fragment C3d (residues 996-1287) which binds to antigens enhancing their uptake by B cells. C3c is another C3b cleavage product residues: 23-664, 749-954, 1321-1663. C3b α and β chains with protein CRIG and Ca+2 ion. Ca+2 ion coordination site (PDB code 2icf). Disease A mutation in CC3 cause the progressive kidney disease: dense deposit disease. Other mutations are associated with recurrent bacterial infections. Relevance Low levels of CC3 in the blood are associated with some kidney diseases.

3D structures of complement C3

Updated on 18-July-2018

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• Complement C3
  • 2icf – hCC3 – human
    
  • 1ghq – hCC3 residues 996-1300 + Epstein-Barr virus receptor
    
  • 4zh1 – hCC3 + complement factor H
    
  • 2b39 – bCC3 – bovine
    
• Complement C3a (anaphylatoxin)
  • 4hw5, 4hwj, 4i6o – hCC3
    
• Complement C3b
  • 2i07, 5fo7 – hCC3 β+α’ chains
    
  • 5fob – hCC3 β+α’ chains + inhibitor
    
  • 5fo9 – hCC3 β+α’ chains + protein
    
  • 5foa, 5f08, 2icf, 2wii – hCC3 α+β chains + protein
    
  • 3g6j, 6ehg – hCC3 α+β chains + antibody
    
  • 5o35 – hCC3 α chain + complement factor H
    
  • 5o32 – hCC3 α chain + complement factor I
    
  • 2xwb – hCC3 α+β chains + complement factor B + complement factor D
    
  • 2xwj – hCC3 α+β chains (mutant) + complement factor B
    
  • 5nbq – hCC3 α chain + complement factor B
    
  • 5fo8 – hCC3 α chain + membrane cofactor protein
    
  • 5m6w – hCC3 α+β chains + complement factor H + complement inhibitor
    
  • 3l5n, 3ohx – hCC3 α+β chains + protein inhibitor
    
  • 2win – hCC3 α+β chains + complement factor B BB fragment + protein inhibitor
    
• Complement C3c
  • 2a74 – hCC3
    
  • 2qki – hCC3 + compstatin
    
  • 3l3o, 3nms – hCC3 + staphylococcal complement inhibitor
    
  • 2ice – hCC3 α+β chains + protein CRIG
    
  • 3t4a – hCC3 α+β chains + fibrinogen-binding protein
    
• Complement C3d
  • 5fcr – CC3 - mouse
    
  • 1c3d – hCC3 (mutant)
    
  • 1w2s, 3oed – hCC3 1-2 sushi domains + complement receptor type 2 precursor
    
  • 2gox, 3d5r, 3d5s – hCC3 α chain fragment + fibrinogen-binding protein
    
  • 2noj – hCC3 α chain fragment (mutant) + EFB homologous protein
    
  • 2wy7, 2wy8 – hCC3 α chain fragment (mutant) + IGG-binding protein
    
  • 3oxu – hCC3 α chain fragment (mutant) + HF protein
    
  • 4m76 – hCC3 α chain fragment (mutant) + integrin α-M
    
  • 2xqw – hCC3 + complement factor H 19-20 sushi domains
    
  • 3rj3 – hCC3 α chain fragment + complement factor H-related protein
    
  • 5mt0, 5mt4, 5tca, 5tcc, 5fbe, 5fbi, 5fck – hCC3 + inhibitor
    
  • 1qqf – rCC3 G fragment - rat
    
  • 1qsj – rCC3 G fragment (mutant)
    

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Michal Harel, Alexander Berchansky