Complement factor

spinqualitylabelsall models Structure of human complement factor H 19-20 sushi domains (magenta) complex with complement C3 (green) and glycerol (PDB code 3oxu). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Complement factor H (CFH) regulates the complement system which is part of the immune response. CFH protects cells by preventing the activation of the complement system when it is not needed. CFH contains 20 short consensus repeats (sushi domains, i.e., a 5 strand β-sandwich arrangement). Complement factor D (CFD) and Complement factor B (CFB) regulate a key step in the activation of the alternative complement pathway. CFD is a member of the chymotrypsin family of serine proteases. Complement factor I (CFI) is a serum protease that inhibits all complement pathways. Disease CFH mutations are involved in dense deposit disease, age-related macular degeneration, atypical hemolytic-uremic syndrome, schizophrenia, stroke and the kidney disorder glomerulonephritis. CFD and CFI are implicated in age-related macular degeneration, . Relevance CFH is recruited by human pathogens resulting in increased virulence. CFB is a novel target for treatment of cardiometabolic disease. Structural highlights The sushi domains are ca. 60 amino acid long containing 2 Cys-Cys bonds.

3D structures of complement factor

Updated on 15-April-2018

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• Complement factor H
  • 1haq, 3gau, 3gav, 3gaw – hCFH – human - NMR
    
  • 2rlp – hCFH 1-2 sushi domains - NMR
    
  • 2rlq – hCFH 2-3 sushi domains - NMR
    
  • 2qfg – hCFH 1-5 sushi domains
    
  • 2yby – mCFH 6-8 sushi domains (mutant) - mouse
    
  • 2ic4 – hCFH 6-8 sushi domains (mutant)
    
  • 2jgw – hCFH 7 sushi domain – NMR
    
  • 2jgx – hCFH 7 sushi domain (mutant)
    
  • 4b2r – hCFH 10-11 sushi domains - NMR
    
  • 4b2s – hCFH 11-12 sushi domains - NMR
    
  • 2kms – hCFH 12-13 sushi domains – NMR
    
  • 1hfi – hCFH 15 sushi domain – NMR
    
  • 1hfh – hCFH 15-16 sushi domains – NMR
    
  • 2qfh – hCFH 16-20 sushi domains - NMR
    
  • 3sw0 – hCFH 18-20 sushi domains
    
  • 2bzm – hCFH 19-20 sushi domains – NMR
    
  • 3kzj – hCFH 19-20 sushi domains (mutant) – NMR
    
  • 2g7i – hCFH 19-20 sushi domains
    
  • 3kxv, 3r62 – hCFH 19-20 sushi domains (mutant)
    
• Complement factor H complexes
  • 2wii – hCFH 1-4 sushi domains + complement C3
    
  • 2w80, 2w81, 4ayd, 4aye, 4ayi, 4aym – hCFH 6-7 sushi domains + factor H binding protein
    
  • 2uwn, 2v8e – hCFH 6-8 sushi domains + sucrose octasulfate
    
  • 4k12 – hCFH 9 sushi domain + choline binding protein A
    
  • 3oxu, 4ont, 4zh1 – hCFH 19-20 sushi domains + complement C3
    
  • 2xqw – hCFH 19-20 sushi domains (mutant) + complement C3
    
  • 4j38 – hCFH 19-20 sushi domains (mutant) + outer surface protein E
    
  • 4k12 – hCFH 9 sushi domain + choline binding protein A
    
  • 5nbq – hCFH + complement C3 a chain + outer surface protein
    
  • 5o32 – hCFH + hCFI + complement C3 a+b chains
    
  • 5o35 – hCFH + complement C3 a chain
    
• Complement factor B
  • 2ok5 – hCFB residues 26-764
    
  • 1dle – hCFB serine protease domain residues 470-764
    
  • 1q0p – hCFB residues 254-476 (mutant)
    
  • 1rrk – hCFB BB fragment residues 243-764 (mutant)
    
• Complement factor B complexes
  • 1rs0 – hCFB BB fragment (mutant) + DIP
    
  • 1rtk – hCFB BB fragment (mutant) + guanidinobenzoate
    
  • 2xwb – hCFB (mutant) + hCFD (mutant) + complement C3B a’+b chains
    
  • 2xwj – hCFB (mutant) + complement C3 a+b chains
    
  • 3hrz, 3hs0 – hCFB (mutant) + cobra venom factor
    
• Complement factor D
  • 1dsu, 1hfd – hCFD
    
  • 1dst, 2xw9, 2xwa, 4cbn, 4cbo – hCFD (mutant)
    
  • 1fdp – hCFD proenzyme
    
• Complement factor D complexes
  • 1bio, 1dfp, 1dic, 5fbe, 5fbi, 5fck, 5fcr, 5mt0, 5mt4, 5nar, 5nat, 5naw, 5nb6, 5nb7, 5nba, 5tca, 5tcc – hCFD + inhibitor
    
  • 4d9r – hCFD + antibody
    
• Complement factor I
  • 2xrc – hCFI
    

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