1or2 - Revision history

OCA at 09:31, 16 August 2023

OCA — Wed, 16 Aug 2023 09:31:07 GMT

←Older revision		Revision as of 09:31, 16 August 2023
Line 3:		Line 3:
	<StructureSection load='1or2' size='340' side='right'caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1or2' size='340' side='right'caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non~~-~~Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [https://pdbe.org/1or2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [https://www.ebi.ac.uk/pdbsum/1or2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or2 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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [https://pdbe.org/1or2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [https://www.ebi.ac.uk/pdbsum/1or2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[https://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[https://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[https://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[https://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[https://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>	+	[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[https://omim.org/entry/107741 107741]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[https://omim.org/entry/104310 104310]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[https://omim.org/entry/269600 269600]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[https://omim.org/entry/611771 611771]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[https://omim.org/entry/143890 143890]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.	+	[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Forstner, M]]	+	[[Category: Forstner M]]
-	[[Category: Rupp, B]]	+	[[Category: Rupp B]]
-	[[Category: Segelke~~, B W]]~~	+	[[Category: Segelke BW]]
-	~~[[Category: Hdl]]~~	+
-	~~[[Category: Heparin-binding]]~~	+
-	~~[[Category: Lipid binding protein]]~~	+
-	~~[[Category: Lipid transport]]~~	+
-	~~[[Category: Plasma protein]]~~	+
-	~~[[Category: Vldl~~]]	+

OCA at 09:20, 8 September 2021

OCA — Wed, 08 Sep 2021 09:20:12 GMT

←Older revision		Revision as of 09:20, 8 September 2021
Line 3:		Line 3:
	<StructureSection load='1or2' size='340' side='right'caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1or2' size='340' side='right'caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [~~http~~://pdbe.org/1or2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1or2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1or2 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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [https://pdbe.org/1or2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [https://www.ebi.ac.uk/pdbsum/1or2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1or2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[~~http~~://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[~~http~~://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[~~http~~://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[~~http~~://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[~~http~~://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>	+	[[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[https://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[https://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[https://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[https://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[https://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.	+	[[https://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 18:38, 20 November 2019

OCA — Wed, 20 Nov 2019 18:38:54 GMT

←Older revision		Revision as of 18:38, 20 November 2019
Line 1:		Line 1:

	==APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165==		==APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165==
-	<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='1or2' size='340' side='right'caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Forstner, M]]		[[Category: Forstner, M]]
	[[Category: Rupp, B]]		[[Category: Rupp, B]]

OCA at 07:48, 15 February 2018

OCA — Thu, 15 Feb 2018 07:48:47 GMT

←Older revision		Revision as of 07:48, 15 February 2018
Line 1:		Line 1:
		+
	==APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165==		==APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165==
	<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://pdbe.org/1or2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://pdbe.org/1or2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1or2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1or2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1or2_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>

OCA at 20:32, 8 February 2016

OCA — Mon, 08 Feb 2016 20:32:37 GMT

←Older revision		Revision as of 20:32, 8 February 2016
Line 18:		Line 18:
	<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=1or2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 15:09, 10 September 2015

OCA — Thu, 10 Sep 2015 15:09:33 GMT

←Older revision		Revision as of 15:09, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://pdbe.org/1or2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	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 1or2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Forstner, M]]		[[Category: Forstner, M]]
	[[Category: Rupp, B]]		[[Category: Rupp, B]]

OCA at 07:16, 6 January 2015

OCA — Tue, 06 Jan 2015 07:16:54 GMT

←Older revision		Revision as of 07:16, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 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=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[http://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[http://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[http://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[http://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>		[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[http://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[http://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[http://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[http://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Forstner, M.]]	+	[[Category: Forstner, M]]
-	[[Category: Rupp, B.]]	+	[[Category: Rupp, B]]
-	[[Category: Segelke, B W.]]	+	[[Category: Segelke, B W]]
	[[Category: Hdl]]		[[Category: Hdl]]
	[[Category: Heparin-binding]]		[[Category: Heparin-binding]]

OCA at 17:04, 29 September 2014

OCA — Mon, 29 Sep 2014 17:04:37 GMT

←Older revision		Revision as of 17:04, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1or2\| PDB=1or2 \| SCENE= }}~~	+	==APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165==
-	===APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165===	+	<StructureSection load='1or2' size='340' side='right' caption='[[1or2]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10850798}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1or2]] 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=1OR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OR2 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[http://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref><ref>PMID:2556398</ref><ref>PMID:1674745</ref><ref>PMID:8287539</ref><ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[http://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[http://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref><ref>PMID:11095479</ref><ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[http://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref><ref>PMID:9176854</ref><ref>PMID:10432380</ref><ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref><ref>PMID:22949395</ref>	+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1or2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1or2 RCSB], [http://www.ebi.ac.uk/pdbsum/1or2 PDBsum]</span></td></tr>
-		+	<table>
-	==Function==	+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[http://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref> <ref>PMID:2556398</ref> <ref>PMID:1674745</ref> <ref>PMID:8287539</ref> <ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[http://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[http://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref> <ref>PMID:11095479</ref> <ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[http://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref> <ref>PMID:9176854</ref> <ref>PMID:10432380</ref> <ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref> <ref>PMID:22949395</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.		[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
		+	== 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/or/1or2_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 ==
		+	An amino-terminal fragment of human apolipoprotein E3 (residues 1-165) has been expressed and crystallized in three different crystal forms under similar crystallization conditions. One crystal form has nearly identical cell dimensions to the previously reported orthorhombic (P2(1)2(1)2(1)) crystal form of the amino-terminal 22 kDa fragment of apolipoprotein E (residues 1-191). A second orthorhombic crystal form (P2(1)2(1)2(1) with cell dimensions differing from the first form) and a trigonal (P3(1)21) crystal form were also characterized. The structures of the first orthorhombic and the trigonal form were determined by seleno-methionine multiwavelength anomalous dispersion, and the structure of the second orthorhombic form was determined by molecular replacement using the structure from the trigonal form as a search model. A combination of modern experimental and computational techniques provided high-quality electron-density maps, which revealed new features of the apolipoprotein E structure, including an unambiguously traced loop connecting helices 2 and 3 in the four-helix bundle and a number of multiconformation side chains. The three crystal forms contain a common intermolecular, antiparallel packing arrangement. The electrostatic complimentarity observed in this antiparallel packing resembles the interaction of apolipoprotein E with the monoclonal antibody 2E8 and the low density lipoprotein receptor. Superposition of the model structures from all three crystal forms reveals flexibility and pronounced kinks in helices near one end of the four-helix bundle. This mobility at one end of the molecule provides new insights into the structural changes in apolipoprotein E that occur with lipid association.

-	~~==About this Structure==~~	+	Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding.,Segelke BW, Forstner M, Knapp M, Trakhanov SD, Parkin S, Newhouse YM, Bellamy HD, Weisgraber KH, Rupp B Protein Sci. 2000 May;9(5):886-97. PMID:10850798<ref>PMID:10850798</ref>
-	~~[[1or2]] 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=1OR2 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:010850798</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Forstner, M.]]		[[Category: Forstner, M.]]

OCA at 21:11, 24 March 2013

OCA — Sun, 24 Mar 2013 21:11:45 GMT

←Older revision		Revision as of 21:11, 24 March 2013
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-	[[Image:1or2.png\|left\|200px]]
-
	{{STRUCTURE_1or2\| PDB=1or2 \| SCENE= }}		{{STRUCTURE_1or2\| PDB=1or2 \| SCENE= }}
-
	===APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165===		===APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165===
		+	{{ABSTRACT_PUBMED_10850798}}

-	~~{{ABSTRACT_PUBMED_10850798}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Defects in APOE are a cause of hyperlipoproteinemia type 3 (HLPP3) [MIM:[http://omim.org/entry/107741 107741]]; also known as familial dysbetalipoproteinemia. Individuals with HLPP3 are clinically characterized by xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The vast majority of the patients are homozygous for APOE2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE4 variant are at higher risk of CAD.<ref>PMID:8346443</ref><ref>PMID:2556398</ref><ref>PMID:1674745</ref><ref>PMID:8287539</ref><ref>PMID:22481068</ref> Genetic variations in APOE are associated with Alzheimer disease type 2 (AD2) [MIM:[http://omim.org/entry/104310 104310]]. It is a late-onset neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. Note=The APOE4 allele is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE4 alleles in 42 families with late onset AD. Thus APOE4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known.<ref>PMID:8346443</ref> Defects in APOE are a cause of sea-blue histiocyte disease (SBHD) [MIM:[http://omim.org/entry/269600 269600]]; also known as sea-blue histiocytosis. This disorder is characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses.<ref>PMID:8346443</ref><ref>PMID:11095479</ref><ref>PMID:16094309</ref> Defects in APOE are a cause of lipoprotein glomerulopathy (LPG) [MIM:[http://omim.org/entry/611771 611771]]. LPG is an uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. It mainly affects people of Japanese and Chinese origin. The disorder has rarely been described in Caucasians.<ref>PMID:8346443</ref><ref>PMID:9176854</ref><ref>PMID:10432380</ref><ref>PMID:18077821</ref> Defects in APOE are a cause of familial hypercholesterolemia (FH) [MIM:[http://omim.org/entry/143890 143890]]. FH is a condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.<ref>PMID:8346443</ref><ref>PMID:22949395</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/APOE_HUMAN APOE_HUMAN]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
-	<ref group="xtra">PMID:010850798</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010850798</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Forstner, M.]]		[[Category: Forstner, M.]]

OCA: Protected "1or2" [edit=sysop:move=sysop]

OCA — Wed, 12 Dec 2012 21:49:20 GMT

Protected "1or2" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:49, 12 December 2012