4enz - Revision history

OCA at 15:05, 14 March 2024

2024-03-14T15:05:51Z

←Older revision		Revision as of 15:05, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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]] 2.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [https://pdbe.org/4enz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [https://www.ebi.ac.uk/pdbsum/4enz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz 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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [https://pdbe.org/4enz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [https://www.ebi.ac.uk/pdbsum/4enz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[https://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.	+	[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[https://omim.org/entry/604290 604290]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).	+	[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Copper-containing ferroxidase ceruloplasmin (Cp) forms binary and ternary complexes with cationic proteins lactoferrin (Lf) and myeloperoxidase (Mpo) during inflammation. We present an X-ray crystal structure of a 2Cp-Mpo complex at 4.7 A resolution. This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo. Small angle X-ray scattering was employed to construct low-resolution models of the Cp-Lf complex and, for the first time, of the ternary 2Cp-2Lf-Mpo complex in solution. The SAXS-based model of Cp-Lf supports the predicted 1:1 stoichiometry of the complex and demonstrates that both lobes of Lf contact domains 1 and 6 of Cp. The 2Cp-2Lf-Mpo SAXS model reveals the absence of interaction between Mpo and Lf in the ternary complex, so Cp can serve as a mediator of protein interactions in complex architecture. Mpo protects antioxidant properties of Cp by isolating its sensitive loop from proteases. The latter is important for incorporation of Fe(3+) into Lf, which activates ferroxidase activity of Cp and precludes oxidation of Cp substrates. Our models provide the structural basis for possible regulatory role of these complexes in preventing iron-induced oxidative damage.	+
-		+
-	Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins.,Samygina VR, Sokolov AV, Bourenkov G, Petoukhov MV, Pulina MO, Zakharova ET, Vasilyev VB, Bartunik H, Svergun DI PLoS One. 2013 Jul 3;8(7):e67145. doi: 10.1371/journal.pone.0067145. Print 2013. PMID:23843990<ref>PMID:23843990</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4enz" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Ceruloplasmin\|Ceruloplasmin]]		*[[Ceruloplasmin\|Ceruloplasmin]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:20, 28 September 2022

2022-09-28T07:20:04Z

←Older revision		Revision as of 07:20, 28 September 2022
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	<StructureSection load='4enz' size='340' side='right'caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4enz' size='340' side='right'caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ejx\|4ejx]]</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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [https://pdbe.org/4enz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [https://www.ebi.ac.uk/pdbsum/4enz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [~~http~~://pdbe.org/4enz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4enz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[~~http~~://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.	+	[[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[https://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).	+	[[https://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bartunik, H]]	+	[[Category: Bartunik H]]
-	[[Category: Bourenkov, G]]	+	[[Category: Bourenkov G]]
-	[[Category: Samygina~~, V R~~]]	+	[[Category: Samygina VR]]
-	[[Category: Sokolov~~, A V~~]]	+	[[Category: Sokolov AV]]
-	[[Category: Vasilyev~~, V B]]~~	+	[[Category: Vasilyev VB]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Plastocyanin-like domain~~]]	+

OCA at 07:22, 27 March 2019

2019-03-27T07:22:05Z

←Older revision		Revision as of 07:22, 27 March 2019
Line 1:		Line 1:

	==Structure of human ceruloplasmin at 2.6 A resolution==		==Structure of human ceruloplasmin at 2.6 A resolution==
-	<StructureSection load='4enz' size='340' side='right' caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='4enz' size='340' side='right'caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
Line 31:		Line 31:
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Bartunik, H]]		[[Category: Bartunik, H]]
	[[Category: Bourenkov, G]]		[[Category: Bourenkov, G]]

OCA at 02:38, 11 December 2016

2016-12-11T02:38:54Z

←Older revision		Revision as of 02:38, 11 December 2016
Line 1:		Line 1:
		+
	==Structure of human ceruloplasmin at 2.6 A resolution==		==Structure of human ceruloplasmin at 2.6 A resolution==
	<StructureSection load='4enz' size='340' side='right' caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4enz' size='340' side='right' caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ejx\|4ejx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ejx\|4ejx]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [http://www.ebi.ac.uk/pdbsum/4enz 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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [http://pdbe.org/4enz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [http://www.ebi.ac.uk/pdbsum/4enz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4enz ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 4enz" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:32, 15 February 2015

2015-02-15T07:32:15Z

←Older revision		Revision as of 07:32, 15 February 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4enz\| PDB=4enz \| SCENE= }}~~	+	==Structure of human ceruloplasmin at 2.6 A resolution==
-	===Structure of human ceruloplasmin at 2.6 A resolution===	+	<StructureSection load='4enz' size='340' side='right' caption='[[4enz]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23843990}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4enz]] 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=4ENZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ENZ FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ejx\|4ejx]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=4enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4enz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4enz RCSB], [http://www.ebi.ac.uk/pdbsum/4enz PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[http://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.		[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[http://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).		[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Copper-containing ferroxidase ceruloplasmin (Cp) forms binary and ternary complexes with cationic proteins lactoferrin (Lf) and myeloperoxidase (Mpo) during inflammation. We present an X-ray crystal structure of a 2Cp-Mpo complex at 4.7 A resolution. This structure allows one to identify major protein-protein interaction areas and provides an explanation for a competitive inhibition of Mpo by Cp and for the activation of p-phenylenediamine oxidation by Mpo. Small angle X-ray scattering was employed to construct low-resolution models of the Cp-Lf complex and, for the first time, of the ternary 2Cp-2Lf-Mpo complex in solution. The SAXS-based model of Cp-Lf supports the predicted 1:1 stoichiometry of the complex and demonstrates that both lobes of Lf contact domains 1 and 6 of Cp. The 2Cp-2Lf-Mpo SAXS model reveals the absence of interaction between Mpo and Lf in the ternary complex, so Cp can serve as a mediator of protein interactions in complex architecture. Mpo protects antioxidant properties of Cp by isolating its sensitive loop from proteases. The latter is important for incorporation of Fe(3+) into Lf, which activates ferroxidase activity of Cp and precludes oxidation of Cp substrates. Our models provide the structural basis for possible regulatory role of these complexes in preventing iron-induced oxidative damage.

-	~~==About this Structure==~~	+	Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins.,Samygina VR, Sokolov AV, Bourenkov G, Petoukhov MV, Pulina MO, Zakharova ET, Vasilyev VB, Bartunik H, Svergun DI PLoS One. 2013 Jul 3;8(7):e67145. doi: 10.1371/journal.pone.0067145. Print 2013. PMID:23843990<ref>PMID:23843990</ref>
-	~~[[4enz]] 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=4ENZ OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Ceruloplasmin\|Ceruloplasmin]]		*[[Ceruloplasmin\|Ceruloplasmin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023843990</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bartunik, H.]]	+	[[Category: Bartunik, H]]
-	[[Category: Bourenkov, G.]]	+	[[Category: Bourenkov, G]]
-	[[Category: Samygina, V R.]]	+	[[Category: Samygina, V R]]
-	[[Category: Sokolov, A V.]]	+	[[Category: Sokolov, A V]]
-	[[Category: Vasilyev, V B.]]	+	[[Category: Vasilyev, V B]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Plastocyanin-like domain]]		[[Category: Plastocyanin-like domain]]

OCA at 04:06, 12 September 2013

2013-09-12T04:06:21Z

←Older revision		Revision as of 04:06, 12 September 2013
Line 1:		Line 1:
	{{STRUCTURE_4enz\| PDB=4enz \| SCENE= }}		{{STRUCTURE_4enz\| PDB=4enz \| SCENE= }}
	===Structure of human ceruloplasmin at 2.6 A resolution===		===Structure of human ceruloplasmin at 2.6 A resolution===
		+	{{ABSTRACT_PUBMED_23843990}}

	==Disease==		==Disease==
Line 10:		Line 11:
	==About this Structure==		==About this Structure==
	[[4enz]] 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=4ENZ OCA].		[[4enz]] 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=4ENZ OCA].
		+
		+	==See Also==
		+	*[[Ceruloplasmin\|Ceruloplasmin]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023843990</ref><references group="xtra"/><references/>
	[[Category: Ferroxidase]]		[[Category: Ferroxidase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 20:32, 17 April 2013

2013-04-17T20:32:31Z

←Older revision		Revision as of 20:32, 17 April 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4enz\| PDB=4enz \| SCENE= }}
		+	===Structure of human ceruloplasmin at 2.6 A resolution===

-	~~The~~ entry ~~4enz~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:[http://omim.org/entry/604290 604290]]. It is an autosomal recessive disorder of iron metabolism characterized by iron accumulation in the brain as well as visceral organs. Clinical features consist of the triad of retinal degeneration, diabetes mellitus and neurological disturbances. Note=Ceruloplasmin levels are decreased in Wilson disease, in which copper cannot be incorporated into ceruloplasmin in liver because of defects in the copper-transporting ATPase 2.

-	~~Authors~~: ~~Samygina, V~~.R., ~~Sokolov, A~~.V.~~, Bourenkov, G~~.~~, Vasilyev, V~~.~~B., Bartunik, H~~.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/CERU_HUMAN CERU_HUMAN]] Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).

-	~~Description:~~ Structure ~~of human ceruloplasmin at 2~~.6 A ~~resolution~~	+	==About this Structure==
		+	[[4enz]] 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=4ENZ OCA].
		+	[[Category: Ferroxidase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Bartunik, H.]]
		+	[[Category: Bourenkov, G.]]
		+	[[Category: Samygina, V R.]]
		+	[[Category: Sokolov, A V.]]
		+	[[Category: Vasilyev, V B.]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Plastocyanin-like domain]]

OCA at 08:57, 21 November 2012

2012-11-21T08:57:06Z

←Older revision		Revision as of 08:57, 21 November 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4enz is ON HOLD	+	The entry 4enz is ON HOLD until Paper Publication

	Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H.		Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H.

	Description: Structure of human ceruloplasmin at 2.6 A resolution		Description: Structure of human ceruloplasmin at 2.6 A resolution

OCA: Protected "4enz" [edit=sysop:move=sysop]

2012-04-25T08:55:03Z

Protected "4enz" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:55, 25 April 2012

OCA: New page: '''Unreleased structure''' The entry 4enz is ON HOLD Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H. Description: Structure of human ceruloplasmin a...

2012-04-25T08:55:02Z

New page: '''Unreleased structure''' The entry 4enz is ON HOLD Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H. Description: Structure of human ceruloplasmin a...

New page

'''Unreleased structure'''

The entry 4enz is ON HOLD

Authors: Samygina, V.R., Sokolov, A.V., Bourenkov, G., Vasilyev, V.B., Bartunik, H.

Description: Structure of human ceruloplasmin at 2.6 A resolution