3kzj - Revision history

OCA at 16:18, 1 November 2023

2023-11-01T16:18:36Z

←Older revision		Revision as of 16:18, 1 November 2023
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	<StructureSection load='3kzj' size='340' side='right'caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='3kzj' size='340' side='right'caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.65Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2g7i\|2g7i]], [[3kxv\|3kxv]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [https://pdbe.org/3kzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [https://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [https://pdbe.org/3kzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [https://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[https://omim.org/entry/126700 126700]]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[https://omim.org/entry/609814 609814]]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref> <ref>PMID:10803850</ref> <ref>PMID:11170895</ref> <ref>PMID:11170896</ref> <ref>PMID:11158219</ref> <ref>PMID:12020532</ref> <ref>PMID:14978182</ref> <ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[https://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref> <ref>PMID:9551389</ref> <ref>PMID:10577907</ref> <ref>PMID:10762557</ref> <ref>PMID:11851332</ref> <ref>PMID:14583443</ref> <ref>PMID:12960213</ref> <ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[https://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>	+	[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[https://omim.org/entry/126700 126700]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[https://omim.org/entry/609814 609814]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref> <ref>PMID:10803850</ref> <ref>PMID:11170895</ref> <ref>PMID:11170896</ref> <ref>PMID:11158219</ref> <ref>PMID:12020532</ref> <ref>PMID:14978182</ref> <ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[https://omim.org/entry/235400 235400]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref> <ref>PMID:9551389</ref> <ref>PMID:10577907</ref> <ref>PMID:10762557</ref> <ref>PMID:11851332</ref> <ref>PMID:14583443</ref> <ref>PMID:12960213</ref> <ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[https://omim.org/entry/610698 610698]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.	+	[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bhattacharjee, A]]	+	[[Category: Bhattacharjee A]]
-	[[Category: Goldman, A]]	+	[[Category: Goldman A]]
-	[[Category: Jokiranta~~, T S~~]]	+	[[Category: Jokiranta TS]]
-	[[Category: Kajander, T]]	+	[[Category: Kajander T]]
-	[[Category: Lehtinen~~, M J]]~~	+	[[Category: Lehtinen MJ]]
-	~~[[Category: Age-related macular degeneration]]~~	+
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Ccp]]~~	+
-	~~[[Category: Complement alternate pathway]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Immune response]]~~	+
-	~~[[Category: Immune system]]~~	+
-	~~[[Category: Innate immunity]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Scr]]~~	+
-	~~[[Category: Secreted]]~~	+
-	~~[[Category: Sushi domain~~]]	+

OCA at 07:52, 10 November 2021

2021-11-10T07:52:16Z

OCA at 07:04, 7 October 2020

2020-10-07T07:04:26Z

←Older revision		Revision as of 07:04, 7 October 2020
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	==Structure of complement Factor H variant R1203A==		==Structure of complement Factor H variant R1203A==
-	<StructureSection load='3kzj' size='340' side='right' caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='3kzj' size='340' side='right'caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [http://pdbe.org/3kzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [http://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [http://pdbe.org/3kzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [http://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Complement factor\|Complement factor]]	+	*[[Complement factor 3D structures\|Complement factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bhattacharjee, A]]		[[Category: Bhattacharjee, A]]
	[[Category: Goldman, A]]		[[Category: Goldman, A]]

OCA at 06:32, 2 January 2019

2019-01-02T06:32:05Z

←Older revision		Revision as of 06:32, 2 January 2019
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/3kzj_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/3kzj_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Complement factor H\|Complement factor H]]	+	*[[Complement factor\|Complement factor]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Lehtinen, M J]]		[[Category: Lehtinen, M J]]
	[[Category: Age-related macular degeneration]]		[[Category: Age-related macular degeneration]]
		+	[[Category: Alternative splicing]]
	[[Category: Ccp]]		[[Category: Ccp]]
	[[Category: Complement alternate pathway]]		[[Category: Complement alternate pathway]]
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	[[Category: Immune system]]		[[Category: Immune system]]
	[[Category: Innate immunity]]		[[Category: Innate immunity]]
		+	[[Category: Polymorphism]]
	[[Category: Scr]]		[[Category: Scr]]
	[[Category: Secreted]]		[[Category: Secreted]]
	[[Category: Sushi domain]]		[[Category: Sushi domain]]

OCA at 12:04, 4 August 2016

2016-08-04T12:04:57Z

←Older revision		Revision as of 12:04, 4 August 2016
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		+
	==Structure of complement Factor H variant R1203A==		==Structure of complement Factor H variant R1203A==
	<StructureSection load='3kzj' size='340' side='right' caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='3kzj' size='340' side='right' caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [http://www.ebi.ac.uk/pdbsum/3kzj PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [http://pdbe.org/3kzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [http://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kzj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3kzj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bhattacharjee, A]]		[[Category: Bhattacharjee, A]]
	[[Category: Goldman, A]]		[[Category: Goldman, A]]

OCA at 14:44, 18 December 2014

2014-12-18T14:44:47Z

←Older revision		Revision as of 14:44, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3kzj~~\| ~~PDB~~=3kzj \| ~~SCENE~~= }}	+	==Structure of complement Factor H variant R1203A==
-	===~~Structure~~ of complement Factor H ~~variant R1203A~~===	+	<StructureSection load='3kzj' size='340' side='right' caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20378178}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [http://www.ebi.ac.uk/pdbsum/3kzj PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[http://omim.org/entry/126700 126700]]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[http://omim.org/entry/609814 609814]]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref> <ref>PMID:10803850</ref> <ref>PMID:11170895</ref> <ref>PMID:11170896</ref> <ref>PMID:11158219</ref> <ref>PMID:12020532</ref> <ref>PMID:14978182</ref> <ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[http://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref> <ref>PMID:9551389</ref> <ref>PMID:10577907</ref> <ref>PMID:10762557</ref> <ref>PMID:11851332</ref> <ref>PMID:14583443</ref> <ref>PMID:12960213</ref> <ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[http://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kz/3kzj_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Factor H (FH) regulates the alternative pathway of complement in plasma and mediates discrimination of cellular surfaces to alternative pathway activators and non-activators. The carboxyl-terminal domains 19 and 20 of FH are essential in target discrimination and are known to contain binding sites for the C3d part of C3b, heparin, and endothelial cells. Mutations in FH19-20 are frequently found in patients with atypical haemolytic uremic syndrome (aHUS). Most aHUS-associated and some other mutations have been shown to lead to impaired binding to C3d and C3b by the recombinant FH19-20 fragment. Most of these mutated residues, such as R1203, are located close to each other in domain 20 but some, such as Q1139, are located in domain 19. We generated mutant proteins Q1139A and R1203A of FH19-20 and showed that their binding to C3d and C3b was clearly impaired. To show that the effects on C3d/C3b binding are due to direct interactions rather than structural changes, we solved the X-ray crystal structures of the R1203A and Q1139A mutant proteins at 1.65 and 2.0A, respectively. Neither of the mutations caused any overall structural changes in FH19-20. It is thus evident that Q1139 in domain 19 and R1203 in domain 20 are directly involved in binding to the C3d part of C3b and therefore both the domains are involved in the interaction with C3d and C3b. This explains why several aHUS-associated FH mutations are found within domain 19 in addition to domain 20.

-	~~==Disease==~~	+	Both domain 19 and domain 20 of factor H are involved in binding to complement C3b and C3d.,Bhattacharjee A, Lehtinen MJ, Kajander T, Goldman A, Jokiranta TS Mol Immunol. 2010 May;47(9):1686-91. Epub 2010 Apr 7. PMID:20378178<ref>PMID:20378178</ref>
-	~~[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[http://omim.org/entry/126700 126700]]; also known as drusen~~ of ~~Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen~~ are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to ~~a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of~~ complement ~~factor H deficiency (CFHD) [MIM:[http://omim.org/entry/609814 609814]]~~. A ~~disorder that can manifest as several different phenotypes~~, ~~including asymptomatic~~, ~~recurrent bacterial infections~~, ~~and renal failure. Laboratory features usually include decreased serum levels of factor H~~, ~~complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway~~. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref><ref>PMID:10803850</ref><ref>PMID:11170895</ref><ref>PMID:11170896</ref><ref>PMID:11158219</ref><ref>PMID:12020532</ref><ref>PMID:14978182</ref><ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (~~AHUS1~~) ~~[MIM~~:[http://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-~~stage renal disease~~. ~~Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system~~. ~~Other genes may play a role in modifying the phenotype.<ref>~~PMID:~~14978182</ref>~~<ref>PMID:~~9551389~~</ref><ref>PMID:10577907</ref><ref>PMID:10762557</ref><ref>PMID:11851332</ref><ref>PMID:14583443</ref><ref>PMID:12960213</ref><ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[http://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>	+
-		+
-	~~==Function==~~	+
-	[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3kzj]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:020378178</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Complement factor H\|Complement factor H]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bhattacharjee, A.]]	+	[[Category: Bhattacharjee, A]]
-	[[Category: Goldman, A.]]	+	[[Category: Goldman, A]]
-	[[Category: Jokiranta, T S.]]	+	[[Category: Jokiranta, T S]]
-	[[Category: Kajander, T.]]	+	[[Category: Kajander, T]]
-	[[Category: Lehtinen, M J.]]	+	[[Category: Lehtinen, M J]]
	[[Category: Age-related macular degeneration]]		[[Category: Age-related macular degeneration]]
	[[Category: Ccp]]		[[Category: Ccp]]

OCA: Protected "3kzj" [edit=sysop:move=sysop]

2013-03-24T18:07:30Z

Protected "3kzj" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:07, 24 March 2013

OCA at 18:07, 24 March 2013

2013-03-24T18:07:28Z

←Older revision		Revision as of 18:07, 24 March 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:3kzj.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3kzj", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3kzj\| PDB=3kzj \| SCENE= }}		{{STRUCTURE_3kzj\| PDB=3kzj \| SCENE= }}
-
	===Structure of complement Factor H variant R1203A===		===Structure of complement Factor H variant R1203A===
		+	{{ABSTRACT_PUBMED_20378178}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[http://omim.org/entry/126700 126700]]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[http://omim.org/entry/609814 609814]]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref><ref>PMID:10803850</ref><ref>PMID:11170895</ref><ref>PMID:11170896</ref><ref>PMID:11158219</ref><ref>PMID:12020532</ref><ref>PMID:14978182</ref><ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[http://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref><ref>PMID:9551389</ref><ref>PMID:10577907</ref><ref>PMID:10762557</ref><ref>PMID:11851332</ref><ref>PMID:14583443</ref><ref>PMID:12960213</ref><ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[http://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_20378178}}, adds the Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~)~~, where 20378178 is~~ the ~~PubMed ID number~~.	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_20378178}}~~	+

	==About this Structure==		==About this Structure==
-	~~3KZJ~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA].	+	[[3kzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20378178~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020378178</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bhattacharjee, A.]]		[[Category: Bhattacharjee, A.]]
Line 31:		Line 21:
	[[Category: Lehtinen, M J.]]		[[Category: Lehtinen, M J.]]
	[[Category: Age-related macular degeneration]]		[[Category: Age-related macular degeneration]]
-	[[Category: Alternative splicing]]
	[[Category: Ccp]]		[[Category: Ccp]]
	[[Category: Complement alternate pathway]]		[[Category: Complement alternate pathway]]
Line 39:		Line 28:
	[[Category: Immune system]]		[[Category: Immune system]]
	[[Category: Innate immunity]]		[[Category: Innate immunity]]
-	[[Category: Polymorphism]]
	[[Category: Scr]]		[[Category: Scr]]
	[[Category: Secreted]]		[[Category: Secreted]]
	[[Category: Sushi domain]]		[[Category: Sushi domain]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:30:20 2010''

OCA at 06:30, 20 May 2010

2010-05-20T06:30:21Z

←Older revision		Revision as of 06:30, 20 May 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3kzj.jpg\|left\|200px]]

-	The ~~entry 3kzj~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3kzj", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3kzj\| PDB=3kzj \| SCENE= }}

-	~~Authors: Bhattacharjee, A., Lehtinen, M.J., Kajander, T., Goldman, A., Jokiranta, T.S.~~	+	===Structure of complement Factor H variant R1203A===

-	Description: Structure of complement Factor H variant R1203A

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 6~~ 09:13:33 2010''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20378178}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20378178 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20378178}}
		+
		+	==About this Structure==
		+	3KZJ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:20378178</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Bhattacharjee, A.]]
		+	[[Category: Goldman, A.]]
		+	[[Category: Jokiranta, T S.]]
		+	[[Category: Kajander, T.]]
		+	[[Category: Lehtinen, M J.]]
		+	[[Category: Age-related macular degeneration]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Ccp]]
		+	[[Category: Complement alternate pathway]]
		+	[[Category: Disease mutation]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Immune response]]
		+	[[Category: Immune system]]
		+	[[Category: Innate immunity]]
		+	[[Category: Polymorphism]]
		+	[[Category: Scr]]
		+	[[Category: Secreted]]
		+	[[Category: Sushi domain]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 20 09:30:20 2010''

OCA at 07:13, 6 January 2010

2010-01-06T07:13:33Z

←Older revision		Revision as of 07:13, 6 January 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3kzj is ON HOLD	+	The entry 3kzj is ON HOLD until Paper Publication

	Authors: Bhattacharjee, A., Lehtinen, M.J., Kajander, T., Goldman, A., Jokiranta, T.S.		Authors: Bhattacharjee, A., Lehtinen, M.J., Kajander, T., Goldman, A., Jokiranta, T.S.
Line 7:		Line 7:
	Description: Structure of complement Factor H variant R1203A		Description: Structure of complement Factor H variant R1203A

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Dec 16 12~~:39:~~53 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 6 09:13:33 2010''

←Older revision		Revision as of 07:52, 10 November 2021
Line 3:		Line 3:
	<StructureSection load='3kzj' size='340' side='right'caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='3kzj' size='340' side='right'caption='[[3kzj]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3kzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZJ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2g7i\|2g7i]], [[3kxv\|3kxv]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g7i\|2g7i]], [[3kxv\|3kxv]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [~~http~~://pdbe.org/3kzj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kzj OCA], [https://pdbe.org/3kzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kzj RCSB], [https://www.ebi.ac.uk/pdbsum/3kzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kzj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[~~http~~://omim.org/entry/126700 126700]]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[~~http~~://omim.org/entry/609814 609814]]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref> <ref>PMID:10803850</ref> <ref>PMID:11170895</ref> <ref>PMID:11170896</ref> <ref>PMID:11158219</ref> <ref>PMID:12020532</ref> <ref>PMID:14978182</ref> <ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[~~http~~://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref> <ref>PMID:9551389</ref> <ref>PMID:10577907</ref> <ref>PMID:10762557</ref> <ref>PMID:11851332</ref> <ref>PMID:14583443</ref> <ref>PMID:12960213</ref> <ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[~~http~~://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>	+	[[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Genetic variations in CFH are associated with basal laminar drusen (BLD) [MIM:[https://omim.org/entry/126700 126700]]; also known as drusen of Bruch membrane or cuticular drusen or grouped early adult-onset drusen. Drusen are extracellular deposits that accumulate below the retinal pigment epithelium on Bruch membrane. Basal laminar drusen refers to an early adult-onset drusen phenotype that shows a pattern of uniform small, slightly raised yellow subretinal nodules randomly scattered in the macula. In later stages, these drusen often become more numerous, with clustered groups of drusen scattered throughout the retina. In time these small basal laminar drusen may expand and ultimately lead to a serous pigment epithelial detachment of the macula that may result in vision loss. Defects in CFH are the cause of complement factor H deficiency (CFHD) [MIM:[https://omim.org/entry/609814 609814]]. A disorder that can manifest as several different phenotypes, including asymptomatic, recurrent bacterial infections, and renal failure. Laboratory features usually include decreased serum levels of factor H, complement component C3, and a decrease in other terminal complement components, indicating activation of the alternative complement pathway. It is associated with a number of renal diseases with variable clinical presentation and progression, including membranoproliferative glomerulonephritis and atypical hemolytic uremic syndrome.<ref>PMID:9312129</ref> <ref>PMID:10803850</ref> <ref>PMID:11170895</ref> <ref>PMID:11170896</ref> <ref>PMID:11158219</ref> <ref>PMID:12020532</ref> <ref>PMID:14978182</ref> <ref>PMID:16612335</ref> Defects in CFH are a cause of susceptibility to hemolytic uremic syndrome atypical type 1 (AHUS1) [MIM:[https://omim.org/entry/235400 235400]]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:14978182</ref> <ref>PMID:9551389</ref> <ref>PMID:10577907</ref> <ref>PMID:10762557</ref> <ref>PMID:11851332</ref> <ref>PMID:14583443</ref> <ref>PMID:12960213</ref> <ref>PMID:20513133</ref> Genetic variation in CFH is associated with age-related macular degeneration type 4 (ARMD4) [MIM:[https://omim.org/entry/610698 610698]]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid (known as drusen) that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.<ref>PMID:22019782</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.	+	[[https://www.uniprot.org/uniprot/CFAH_HUMAN CFAH_HUMAN]] Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]