Complement factor

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The <scene name='59/594535/Cv/5'>sushi domains are ca. 60 amino acid long containing 2 Cys-Cys bonds</scene>.
The <scene name='59/594535/Cv/5'>sushi domains are ca. 60 amino acid long containing 2 Cys-Cys bonds</scene>.
*<scene name='59/594535/Cv/6'>Cys-Cys bonds</scene>.
*<scene name='59/594535/Cv/6'>Cys-Cys bonds</scene>.
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==3D structures of complement factor==
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[[Complement factor 3D structures]]
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</StructureSection>
</StructureSection>
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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*Complement factor B
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**[[2ok5]] – hCFB residues 26-764<br />
 +
**[[1dle]] – hCFB serine protease domain residues 470-764<br />
 +
**[[1q0p]] – hCFB residues 254-476 (mutant) <br />
 +
**[[1rrk]] – hCFB BB fragment residues 243-764 (mutant) <br />
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 +
*Complement factor B complexes
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**[[1rs0]] – hCFB BB fragment (mutant) + DIP<br />
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**[[1rtk]] – hCFB BB fragment (mutant) + guanidinobenzoate<br />
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**[[5m6w]] – hCFB + complement C3 α+β chains<br />
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**[[2xwj]] – hCFB (mutant) + complement C3 α+β chains<br />
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**[[2xwb]] – hCFB (mutant) + hCFD (mutant) + complement C3 α+β chains<br />
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**[[3hrz]], [[3hs0]] – hCFB (mutant) + cobra venom factor<br />
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*Complement factor D
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**[[1dsu]], [[1hfd]] – hCFD <br />
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**[[1dst]], [[2xw9]], [[2xwa]], [[4cbn]], [[4cbo]] – hCFD (mutant) <br />
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**[[1fdp]] – hCFD proenzyme <br />
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*Complement factor D complexes
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**[[1bio]], [[1dfp]], [[1dic]], [[5fbe]], [[5fbi]], [[5fck]], [[5fcr]], [[5mt0]], [[5mt4]], [[5nar]], [[5nat]], [[5naw]], [[5nb6]], [[5nb7]], [[5nba]], [[5tca]], [[5tcc]],[[6qmr]], [[6qmt]], [[6fut]], [[6fuj]], [[6fui]], [[6fuh]], [[6fug]], [[6ftz]], [[6fty]] – hCFD + inhibitor <br />
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**[[4d9r]] – hCFD + antibody<br />
*Complement factor H
*Complement factor H
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**[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />
**[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />
**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
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**[[5nbq]] – hCFH + complement C3 a chain + outer surface protein<br />
+
**[[5nbq]] – hCFH + complement C3 α chain + outer surface protein<br />
-
**[[5o32]] – hCFH + hCFI + complement C3 a+b chains <br />
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**[[5o32]] – hCFH + hCFI + complement C3 α+β chains <br />
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**[[5o35]] – hCFH + complement C3 a chain <br />
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**[[5o35]] – hCFH + complement C3 α chain <br />
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+
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*Complement factor B
+
-
 
+
-
**[[2ok5]] – hCFB residues 26-764<br />
+
-
**[[1dle]] – hCFB serine protease domain residues 470-764<br />
+
-
**[[1q0p]] – hCFB residues 254-476 (mutant) <br />
+
-
**[[1rrk]] – hCFB BB fragment residues 243-764 (mutant) <br />
+
-
 
+
-
*Complement factor B complexes
+
-
 
+
-
**[[1rs0]] – hCFB BB fragment (mutant) + DIP<br />
+
-
**[[1rtk]] – hCFB BB fragment (mutant) + guanidinobenzoate<br />
+
-
**[[2xwb]] – hCFB (mutant) + hCFD (mutant) + complement C3B a’+b chains<br />
+
-
**[[2xwj]] – hCFB (mutant) + complement C3 a+b chains<br />
+
-
**[[3hrz]], [[3hs0]] – hCFB (mutant) + cobra venom factor<br />
+
-
 
+
-
*Complement factor D
+
-
 
+
-
**[[1dsu]], [[1hfd]] – hCFD <br />
+
-
**[[1dst]], [[2xw9]], [[2xwa]], [[4cbn]], [[4cbo]] – hCFD (mutant) <br />
+
-
**[[1fdp]] – hCFD proenzyme <br />
+
-
 
+
-
*Complement factor D complexes
+
-
 
+
-
**[[1bio]], [[1dfp]], [[1dic]], [[5fbe]], [[5fbi]], [[5fck]], [[5fcr]], [[5mt0]], [[5mt4]], [[5nar]], [[5nat]], [[5naw]], [[5nb6]], [[5nb7]], [[5nba]], [[5tca]], [[5tcc]] – hCFD + inhibitor <br />
+
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**[[4d9r]] – hCFD + antibody<br />
+
*Complement factor I
*Complement factor I

Revision as of 08:07, 15 May 2019

Structure of human complement factor H 19-20 sushi domains (magenta) complex with complement C3 (green) and glycerol (PDB code 3oxu).

Drag the structure with the mouse to rotate

3D structures of complement factor

Updated on 15-May-2019



References

  1. ↑ Rodriguez de Cordoba S, Esparza-Gordillo J, Goicoechea de Jorge E, Lopez-Trascasa M, Sanchez-Corral P. The human complement factor H: functional roles, genetic variations and disease associations. Mol Immunol. 2004 Jun;41(4):355-67. PMID:15163532 doi:10.1016/j.molimm.2004.02.005
  2. ↑ Stanton CM, Yates JR, den Hollander AI, Seddon JM, Swaroop A, Stambolian D, Fauser S, Hoyng C, Yu Y, Atsuhiro K, Branham K, Othman M, Chen W, Kortvely E, Chalmers K, Hayward C, Moore AT, Dhillon B, Ueffing M, Wright AF. Complement factor D in age-related macular degeneration. Invest Ophthalmol Vis Sci. 2011 Nov 11;52(12):8828-34. doi: 10.1167/iovs.11-7933. PMID:22003108 doi:http://dx.doi.org/10.1167/iovs.11-7933
  3. ↑ Alexander P, Gibson J, Cree AJ, Ennis S, Lotery AJ. Complement factor I and age-related macular degeneration. Mol Vis. 2014 Sep 13;20:1253-7. eCollection 2014. PMID:25352734
  4. ↑ Coan PM, Barrier M, Alfazema N, Carter RN, Marion de Proce S, Dopico XC, Garcia Diaz A, Thomson A, Jackson-Jones LH, Moyon B, Webster Z, Ross D, Moss J, Arends MJ, Morton NM, Aitman TJ. Complement Factor B Is a Determinant of Both Metabolic and Cardiovascular Features of Metabolic Syndrome. Hypertension. 2017 Jul 24. pii: HYPERTENSIONAHA.117.09242. doi:, 10.1161/HYPERTENSIONAHA.117.09242. PMID:28739975 doi:http://dx.doi.org/10.1161/HYPERTENSIONAHA.117.09242

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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