5hk1 - Revision history

OCA at 12:32, 6 March 2024

OCA — Wed, 06 Mar 2024 12:32:43 GMT

←Older revision		Revision as of 12:32, 6 March 2024
Line 12:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN] Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity).[UniProtKB:O55242]<ref>PMID:16472803</ref> <ref>PMID:9341151</ref>		[https://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN] Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity).[UniProtKB:O55242]<ref>PMID:16472803</ref> <ref>PMID:9341151</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The human sigma1 receptor is an enigmatic endoplasmic-reticulum-resident transmembrane protein implicated in a variety of disorders including depression, drug addiction, and neuropathic pain. Recently, an additional connection to amyotrophic lateral sclerosis has emerged from studies of human genetics and mouse models. Unlike many transmembrane receptors that belong to large, extensively studied families such as G-protein-coupled receptors or ligand-gated ion channels, the sigma1 receptor is an evolutionary isolate with no discernible similarity to any other human protein. Despite its increasingly clear importance in human physiology and disease, the molecular architecture of the sigma1 receptor and its regulation by drug-like compounds remain poorly defined. Here we report crystal structures of the human sigma1 receptor in complex with two chemically divergent ligands, PD144418 and 4-IBP. The structures reveal a trimeric architecture with a single transmembrane domain in each protomer. The carboxy-terminal domain of the receptor shows an extensive flat, hydrophobic membrane-proximal surface, suggesting an intimate association with the cytosolic surface of the endoplasmic reticulum membrane in cells. This domain includes a cupin-like beta-barrel with the ligand-binding site buried at its centre. This large, hydrophobic ligand-binding cavity shows remarkable plasticity in ligand recognition, binding the two ligands in similar positions despite dissimilar chemical structures. Taken together, these results reveal the overall architecture, oligomerization state, and molecular basis for ligand recognition by this important but poorly understood protein.
-
-	Crystal structure of the human sigma1 receptor.,Schmidt HR, Zheng S, Gurpinar E, Koehl A, Manglik A, Kruse AC Nature. 2016 Apr 28;532(7600):527-30. doi: 10.1038/nature17391. Epub 2016 Apr 4. PMID:27042935<ref>PMID:27042935</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5hk1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:39, 9 August 2023

OCA — Wed, 09 Aug 2023 07:39:32 GMT

←Older revision		Revision as of 07:39, 9 August 2023
Line 1:		Line 1:

	==Human sigma-1 receptor bound to PD144418==		==Human sigma-1 receptor bound to PD144418==
-	<StructureSection load='5hk1' size='340' side='right' caption='[[5hk1]], [[Resolution\|resolution]] 2.51Å' scene=''>	+	<StructureSection load='5hk1' size='340' side='right'caption='[[5hk1]], [[Resolution\|resolution]] 2.51Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5hk1]] is a 3 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=5HK1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5HK1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5hk1]] is a 3 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=5HK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HK1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=61W:3-(4-METHYLPHENYL)-5-(1-PROPYL-3,6-DIHYDRO-2H-PYRIDIN-5-YL)-1,2-OXAZOLE'>61W</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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]] 2.5051Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SIGMAR1, OPRS1, SRBP, AAG8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=61W:3-(4-METHYLPHENYL)-5-(1-PROPYL-3,6-DIHYDRO-2H-PYRIDIN-5-YL)-1,2-OXAZOLE'>61W</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5hk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk1 OCA], [~~http~~://pdbe.org/5hk1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5hk1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5hk1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk1 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=5hk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk1 OCA], [https://pdbe.org/5hk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hk1 RCSB], [https://www.ebi.ac.uk/pdbsum/5hk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN]] Juvenile amyotrophic lateral sclerosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN] Juvenile amyotrophic lateral sclerosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN]] Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity).[UniProtKB:O55242]<ref>PMID:16472803</ref> <ref>PMID:9341151</ref>	+	[https://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN] Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity).[UniProtKB:O55242]<ref>PMID:16472803</ref> <ref>PMID:9341151</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Gurpinar, E]]	+	[[Category: Large Structures]]
-	[[Category: Koehl, A]]	+	[[Category: Gurpinar E]]
-	[[Category: Kruse~~, A C~~]]	+	[[Category: Koehl A]]
-	[[Category: Manglik, A]]	+	[[Category: Kruse AC]]
-	[[Category: Schmidt~~, H R~~]]	+	[[Category: Manglik A]]
-	[[Category: Zheng, S]]	+	[[Category: Schmidt HR]]
-	~~[[Category: Membrane protein]]~~	+	[[Category: Zheng S]]
-	~~[[Category: Sigma-1 receptor]]~~	+
-	~~[[Category: Signal transduction]]~~	+
-	~~[[Category: Transmembrane receptor~~]]	+

OCA at 13:29, 16 November 2017

OCA — Thu, 16 Nov 2017 13:29:56 GMT

←Older revision		Revision as of 13:29, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5hk1' size='340' side='right' caption='[[5hk1]], [[Resolution\|resolution]] 2.51Å' scene=''>		<StructureSection load='5hk1' size='340' side='right' caption='[[5hk1]], [[Resolution\|resolution]] 2.51Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5hk1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HK1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5hk1]] is a 3 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=5HK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HK1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=61W:3-(4-METHYLPHENYL)-5-(1-PROPYL-3,6-DIHYDRO-2H-PYRIDIN-5-YL)-1,2-OXAZOLE'>61W</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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=61W:3-(4-METHYLPHENYL)-5-(1-PROPYL-3,6-DIHYDRO-2H-PYRIDIN-5-YL)-1,2-OXAZOLE'>61W</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk1 OCA], [http://pdbe.org/5hk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk1 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk1 PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SIGMAR1, OPRS1, SRBP, AAG8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5hk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk1 OCA], [http://pdbe.org/5hk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk1 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Gurpinar, E]]		[[Category: Gurpinar, E]]
	[[Category: Koehl, A]]		[[Category: Koehl, A]]

OCA at 16:17, 10 May 2016

OCA — Tue, 10 May 2016 16:17:26 GMT

←Older revision		Revision as of 16:17, 10 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~5hk1~~ is ~~ON HOLD~~	+	==Human sigma-1 receptor bound to PD144418==
		+	<StructureSection load='5hk1' size='340' side='right' caption='[[5hk1]], [[Resolution\|resolution]] 2.51Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5hk1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HK1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=61W:3-(4-METHYLPHENYL)-5-(1-PROPYL-3,6-DIHYDRO-2H-PYRIDIN-5-YL)-1,2-OXAZOLE'>61W</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk1 OCA], [http://pdbe.org/5hk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk1 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk1 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN]] Juvenile amyotrophic lateral sclerosis. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SGMR1_HUMAN SGMR1_HUMAN]] Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria (By similarity).[UniProtKB:O55242]<ref>PMID:16472803</ref> <ref>PMID:9341151</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The human sigma1 receptor is an enigmatic endoplasmic-reticulum-resident transmembrane protein implicated in a variety of disorders including depression, drug addiction, and neuropathic pain. Recently, an additional connection to amyotrophic lateral sclerosis has emerged from studies of human genetics and mouse models. Unlike many transmembrane receptors that belong to large, extensively studied families such as G-protein-coupled receptors or ligand-gated ion channels, the sigma1 receptor is an evolutionary isolate with no discernible similarity to any other human protein. Despite its increasingly clear importance in human physiology and disease, the molecular architecture of the sigma1 receptor and its regulation by drug-like compounds remain poorly defined. Here we report crystal structures of the human sigma1 receptor in complex with two chemically divergent ligands, PD144418 and 4-IBP. The structures reveal a trimeric architecture with a single transmembrane domain in each protomer. The carboxy-terminal domain of the receptor shows an extensive flat, hydrophobic membrane-proximal surface, suggesting an intimate association with the cytosolic surface of the endoplasmic reticulum membrane in cells. This domain includes a cupin-like beta-barrel with the ligand-binding site buried at its centre. This large, hydrophobic ligand-binding cavity shows remarkable plasticity in ligand recognition, binding the two ligands in similar positions despite dissimilar chemical structures. Taken together, these results reveal the overall architecture, oligomerization state, and molecular basis for ligand recognition by this important but poorly understood protein.

-	~~Authors:~~ Schmidt~~, H.R.~~, Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., Kruse~~, A~~.C.	+	Crystal structure of the human sigma1 receptor.,Schmidt HR, Zheng S, Gurpinar E, Koehl A, Manglik A, Kruse AC Nature. 2016 Apr 28;532(7600):527-30. doi: 10.1038/nature17391. Epub 2016 Apr 4. PMID:27042935<ref>PMID:27042935</ref>

-	~~Description:~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category: Zheng~~, S]]	+	<div class="pdbe-citations 5hk1" style="background-color:#fffaf0;"></div>
-	~~[[Category~~: ~~Schmidt, H.R]]~~	+	== References ==
-	~~[[Category: Koehl, A]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Gurpinar, E]]		[[Category: Gurpinar, E]]
		+	[[Category: Koehl, A]]
		+	[[Category: Kruse, A C]]
	[[Category: Manglik, A]]		[[Category: Manglik, A]]
-	[[Category: ~~Kruse~~, ~~A.C~~]]	+	[[Category: Schmidt, H R]]
		+	[[Category: Zheng, S]]
		+	[[Category: Membrane protein]]
		+	[[Category: Sigma-1 receptor]]
		+	[[Category: Signal transduction]]
		+	[[Category: Transmembrane receptor]]

OCA: Protected "5hk1" [edit=sysop:move=sysop]

OCA — Wed, 20 Jan 2016 15:37:11 GMT

Protected "5hk1" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:37, 20 January 2016

OCA: New page: '''Unreleased structure''' The entry 5hk1 is ON HOLD Authors: Schmidt, H.R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., Kruse, A.C. Description: [[Category: Unreleased Structure...

OCA — Wed, 20 Jan 2016 15:37:10 GMT

New page: '''Unreleased structure''' The entry 5hk1 is ON HOLD Authors: Schmidt, H.R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., Kruse, A.C. Description: [[Category: Unreleased Structure...

New page

'''Unreleased structure'''

The entry 5hk1 is ON HOLD

Authors: Schmidt, H.R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., Kruse, A.C.

Description:
[[Category: Unreleased Structures]]
[[Category: Zheng, S]]
[[Category: Schmidt, H.R]]
[[Category: Koehl, A]]
[[Category: Gurpinar, E]]
[[Category: Manglik, A]]
[[Category: Kruse, A.C]]