Complement factor - Revision history

Michal Harel at 07:05, 6 June 2024

2024-06-06T07:05:37Z

← Older revision		Revision as of 07:05, 6 June 2024
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	== Function ==		== 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)<ref>PMID:15163532</ref>. '''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. '''Complement factor P''' (CFP) is a positive regulator of the alternative complement pathway<ref>PMID:28480349</ref>.		*'''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)<ref>PMID:15163532</ref>.
			*'''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.
			*'''Complement factor P''' (CFP) is a positive regulator of the alternative complement pathway<ref>PMID:28480349</ref>.
	== Disease ==		== Disease ==

Michal Harel at 07:52, 7 July 2020

2020-07-07T07:52:49Z

← Older revision		Revision as of 07:52, 7 July 2020
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	== Function ==		== 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)<ref>PMID:15163532</ref>. '''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.		'''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)<ref>PMID:15163532</ref>. '''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. '''Complement factor P''' (CFP) is a positive regulator of the alternative complement pathway<ref>PMID:28480349</ref>.
	== Disease ==		== Disease ==

Michal Harel at 08:08, 15 May 2019

2019-05-15T08:08:18Z

← Older revision		Revision as of 08:08, 15 May 2019
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	</StructureSection>		</StructureSection>

	~~==3D structures of complement factor==~~

	~~Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}~~
	~~{{#tree:id=OrganizedByTopic\|openlevels=0\|~~

	*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 />
	**[[5m6w]] – hCFB + complement C3 α+β chains<br />
	**[[2xwj]] – hCFB (mutant) + complement C3 α+β chains<br />
	**[[2xwb]] – hCFB (mutant) + hCFD (mutant) + complement C3 α+β 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]],[[6qmr]], [[6qmt]], [[6fut]], [[6fuj]], [[6fui]], [[6fuh]], [[6fug]], [[6ftz]], [[6fty]] – hCFD + inhibitor <br />
	**[[4d9r]] – hCFD + antibody<br />

	*Complement factor H

	**[[1haq]], [[3gau]], [[3gav]], [[3gaw]] – hCFH – human - NMR<br />
	**[[2rlp]] – hCFH 1-2 sushi domains - NMR <br />
	**[[2rlq]] – hCFH 2-3 sushi domains - NMR <br />
	**[[2qfg]] – hCFH 1-5 sushi domains <br />
	**[[2yby]] – mCFH 6-8 sushi domains (mutant) - mouse<br />
	**[[2ic4]] – hCFH 6-8 sushi domains (mutant) <br />
	**[[2jgw]] – hCFH 7 sushi domain – NMR<br />
	**[[2jgx]] – hCFH 7 sushi domain (mutant) <br />
	**[[4b2r]] – hCFH 10-11 sushi domains - NMR <br />
	**[[4b2s]] – hCFH 11-12 sushi domains - NMR <br />
	**[[2kms]] – hCFH 12-13 sushi domains – NMR<br />
	**[[1hfi]] – hCFH 15 sushi domain – NMR<br />
	**[[1hfh]] – hCFH 15-16 sushi domains – NMR<br />
	**[[2qfh]] – hCFH 16-20 sushi domains - NMR <br />
	**[[3sw0]] – hCFH 18-20 sushi domains <br />
	**[[2bzm]] – hCFH 19-20 sushi domains – NMR<br />
	**[[3kzj]] – hCFH 19-20 sushi domains (mutant) – NMR<br />
	**[[2g7i]] – hCFH 19-20 sushi domains <br />
	**[[3kxv]], [[3r62]] – hCFH 19-20 sushi domains (mutant) <br />

	*Complement factor H complexes

	**[[2wii]] – hCFH 1-4 sushi domains + complement C3 <br />
	**[[2w80]], [[2w81]], [[4ayd]], [[4aye]], [[4ayi]], [[4aym]] – hCFH 6-7 sushi domains + factor H binding protein <br />
	**[[2uwn]], [[2v8e]] – hCFH 6-8 sushi domains + sucrose octasulfate <br />
	**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
	**[[3oxu]], [[4ont]], [[4zh1]] – hCFH 19-20 sushi domains + complement C3 <br />
	**[[2xqw]] – hCFH 19-20 sushi domains (mutant) + complement C3 <br />
	**[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />
	**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
	**[[5nbq]] – hCFH + complement C3 α chain + outer surface protein<br />
	**[[5o32]] – hCFH + hCFI + complement C3 α+β chains <br />
	**[[5o35]] – hCFH + complement C3 α chain <br />

	*Complement factor I

	**[[2xrc]] – hCFI <br />

	}}




	== References ==		== References ==

Michal Harel at 08:07, 15 May 2019

2019-05-15T08:07:02Z

@@ Line 16: / Line 16: @@
 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>.
 </StructureSection>
@@ Line 22: / Line 26: @@
 Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 {{#tree:id=OrganizedByTopic|openlevels=0|
 *Complement factor H
@@ Line 55: / Line 86: @@
 **[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />
 **[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
-**[[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 />
+**[[5o32]] – hCFH + hCFI + complement C3 α+β chains <br />
-**[[5o35]] – hCFH + complement C3 a chain <br />
+**[[5o35]] – hCFH + complement C3 α chain <br />
 *Complement factor I

Alexander Berchansky at 06:48, 18 February 2019

2019-02-18T06:48:23Z

← Older revision		Revision as of 06:48, 18 February 2019
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	== Structural highlights ==		== Structural highlights ==

	The <scene name='59/594535/Cv/3'>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/4'>Cys-Cys bonds</scene>.		*<scene name='59/594535/Cv/6'>Cys-Cys bonds</scene>.
	</StructureSection>		</StructureSection>

Alexander Berchansky at 12:59, 16 April 2018

2018-04-16T12:59:58Z

← Older revision		Revision as of 12:59, 16 April 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==

	The <scene name='59/594535/Cv/2'>sushi domains are ca. 60 amino acid long containing 2 Cys-Cys bonds</scene>.		The <scene name='59/594535/Cv/3'>sushi domains are ca. 60 amino acid long containing 2 Cys-Cys bonds</scene>.
			*<scene name='59/594535/Cv/4'>Cys-Cys bonds</scene>.
	</StructureSection>		</StructureSection>

Jaime Prilusky: Complement factor H moved to Complement factor: requested by Editor

2018-04-15T08:31:45Z

Complement factor H moved to Complement factor: requested by Editor

← Older revision	Revision as of 08:31, 15 April 2018
(No difference)

Michal Harel at 08:24, 15 April 2018

2018-04-15T08:24:17Z

← Older revision		Revision as of 08:24, 15 April 2018
Line 3:		Line 3:
	== Function ==		== 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).<ref>PMID:15163532</ref>		'''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)<ref>PMID:15163532</ref>. '''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 ==		== Disease ==

	CFH mutations are involved in dense deposit disease, age-related macular degeneration, atypical hemolytic-uremic syndrome, schizophrenia, stroke and the kidney disorder glomerulonephritis.		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<ref>PMID:22003108</ref>, <ref>PMID:25352734</ref>.

	== Relevance ==		== Relevance ==

	CFH is recruited by human pathogens resulting in increased virulence.		CFH is recruited by human pathogens resulting in increased virulence. CFB is a novel target for treatment of cardiometabolic disease<ref>PMID:28739975</ref>.

	== Structural highlights ==		== Structural highlights ==

Michal Harel at 08:01, 15 April 2018

2018-04-15T08:01:14Z

@@ Line 18: / Line 18: @@
 </StructureSection>
-==3D structures of complement factor H==
+==3D structures of complement factor==
 Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
@@ Line 55: / Line 55: @@
 **[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />
 **[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
 }}

Michal Harel at 09:04, 4 April 2017

2017-04-04T09:04:46Z

← Older revision		Revision as of 09:04, 4 April 2017
Line 51:		Line 51:
	**[[2uwn]], [[2v8e]] – hCFH 6-8 sushi domains + sucrose octasulfate <br />		**[[2uwn]], [[2v8e]] – hCFH 6-8 sushi domains + sucrose octasulfate <br />
	**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />		**[[4k12]] – hCFH 9 sushi domain + choline binding protein A <br />
	**[[3oxu]], [[4ont]] – hCFH 19-20 sushi domains + complement C3 <br />		**[[3oxu]], [[4ont]], [[4zh1]] – hCFH 19-20 sushi domains + complement C3 <br />
	**[[2xqw]] – hCFH 19-20 sushi domains (mutant) + complement C3 <br />		**[[2xqw]] – hCFH 19-20 sushi domains (mutant) + complement C3 <br />
	**[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />		**[[4j38]] – hCFH 19-20 sushi domains (mutant) + outer surface protein E <br />