3l3n - Revision history

OCA at 08:29, 6 September 2023

OCA — Wed, 06 Sep 2023 08:29:32 GMT

←Older revision		Revision as of 08:29, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3l3n' size='340' side='right'caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3l3n' size='340' side='right'caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L3N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L3N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW~~</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC~~</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.3Å</td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;~~'>~~[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]~~</~~div~~>~~</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [https://pdbe.org/3l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [https://www.ebi.ac.uk/pdbsum/3l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3n 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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [https://pdbe.org/3l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [https://www.ebi.ac.uk/pdbsum/3l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3n ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[https://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[https://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>	+	[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[https://omim.org/entry/612624 612624]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[https://omim.org/entry/614519 614519]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.	+	[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kroger~~, W L~~]]	+	[[Category: Kroger WL]]
-	[[Category: ~~Neil, H G.~~O]]	+	[[Category: O'Neil HG]]
-	[[Category: Sewell~~, B T~~]]	+	[[Category: Sewell BT]]
-	[[Category: Sturrock~~, E D~~]]	+	[[Category: Sturrock ED]]
-	[[Category: Watermeyer~~, J M]]~~	+	[[Category: Watermeyer JM]]
-	~~[[Category: Carboxypeptidase]]~~	+
-	~~[[Category: Enzyme-inhibitor complex]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Testis~~]]	+

OCA at 12:31, 13 October 2021

OCA — Wed, 13 Oct 2021 12:31:32 GMT

←Older revision		Revision as of 12:31, 13 October 2021
Line 1:		Line 1:

	==Testis ACE co-crystal structure with novel inhibitor lisW==		==Testis ACE co-crystal structure with novel inhibitor lisW==
-	<StructureSection load='3l3n' size='340' side='right' caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3l3n' size='340' side='right'caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3L3N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L3N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL~~</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC~~</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL-D~~-~~GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=ZN:~~ZINC+ION~~'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([https://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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [~~http~~://pdbe.org/3l3n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3l3n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3n 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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [https://pdbe.org/3l3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [https://www.ebi.ac.uk/pdbsum/3l3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3n ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[~~http~~://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[~~http~~://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[~~http~~://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[~~http~~://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>	+	[[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[https://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[https://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[https://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.	+	[[https://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/3l3n_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/3l3n_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3l3n" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3l3n" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]
		+	*[[Carboxypeptidase 3D structures\|Carboxypeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 41:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Kroger, W L]]		[[Category: Kroger, W L]]
	[[Category: Neil, H G.O]]		[[Category: Neil, H G.O]]

OCA at 08:46, 1 November 2017

OCA — Wed, 01 Nov 2017 08:46:44 GMT

←Older revision		Revision as of 08:46, 1 November 2017
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3N FirstGlance]. <br>		<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=ZN:~~ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA~~-L-~~FUCOSE~~'>~~FUC~~</scene>, <scene name='pdbligand=~~NAG~~:~~N-ACETYL-D-GLUCOSAMINE~~'>~~NAG~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3l3n" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3l3n" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Angiotensin-Converting Enzyme\|Angiotensin-Converting Enzyme]]
-	*[[Carboxypeptidase\|Carboxypeptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 00:15, 5 August 2016

OCA — Fri, 05 Aug 2016 00:15:20 GMT

←Older revision		Revision as of 00:15, 5 August 2016
Line 1:		Line 1:
		+
	==Testis ACE co-crystal structure with novel inhibitor lisW==		==Testis ACE co-crystal structure with novel inhibitor lisW==
	<StructureSection load='3l3n' size='340' side='right' caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3l3n' size='340' side='right' caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3N FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [http://www.ebi.ac.uk/pdbsum/3l3n 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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [http://pdbe.org/3l3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [http://www.ebi.ac.uk/pdbsum/3l3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l3n ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<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=3l3n ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	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 3l3n" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
		+	*[[Angiotensin-Converting Enzyme\|Angiotensin-Converting Enzyme]]
	*[[Carboxypeptidase\|Carboxypeptidase]]		*[[Carboxypeptidase\|Carboxypeptidase]]
	== References ==		== References ==
Line 37:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Kroger, W L]]		[[Category: Kroger, W L]]
	[[Category: Neil, H G.O]]		[[Category: Neil, H G.O]]

OCA at 16:48, 18 December 2014

OCA — Thu, 18 Dec 2014 16:48:43 GMT

←Older revision		Revision as of 16:48, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3l3n\| PDB=3l3n \| SCENE= }}~~	+	==Testis ACE co-crystal structure with novel inhibitor lisW==
-	===Testis ACE co-crystal structure with novel inhibitor lisW===	+	<StructureSection load='3l3n' size='340' side='right' caption='[[3l3n]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20233165}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3l3n]] 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=3L3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3N FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LSW:N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-TRYPTOPHAN'>LSW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o86\|1o86]], [[1o8a\|1o8a]], [[1uze\|1uze]], [[1uzf\|1uzf]], [[2iul\|2iul]], [[3bkk\|3bkk]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ACE, DCP, DCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3l3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l3n RCSB], [http://www.ebi.ac.uk/pdbsum/3l3n PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[http://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[http://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[http://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.
		+	== 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/l3/3l3n_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 ==
		+	Human ACE (angiotensin-converting enzyme) (EC 3.4.15.1) is an important drug target because of its role in the regulation of blood pressure via the renin-angiotensin-aldosterone system. Somatic ACE comprises two homologous domains, the differing substrate preferences of which present a new avenue for domain-selective inhibitor design. We have co-crystallized lisW-S, a C-domain-selective derivative of the drug lisinopril, with human testis ACE and determined a structure using X-ray crystallography to a resolution of 2.30 A (1 A=0.1 nm). In this structure, lisW-S is seen to have a similar binding mode to its parent compound lisinopril, but the P2' tryptophan moiety takes a different conformation to that seen in other inhibitors having a tryptophan residue in this position. We have examined further the domain-specific interactions of this inhibitor by mutating C-domain-specific active-site residues to their N domain equivalents, then assessing the effect of the mutation on inhibition by lisW-S using a fluorescence-based assay. Kinetics analysis shows a 258-fold domain-selectivity that is largely due to the co-operative effect of C-domain-specific residues in the S2' subsite. The high affinity and selectivity of this inhibitor make it a good lead candidate for cardiovascular drug development.

-	~~==Disease==~~	+	Characterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinopril.,Watermeyer JM, Kroger WL, O'Neill HG, Sewell BT, Sturrock ED Biochem J. 2010 Apr 28;428(1):67-74. PMID:20233165<ref>PMID:20233165</ref>
-	~~[[http://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations~~ in ~~ACE may be~~ a ~~cause~~ of ~~susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim~~.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, ~~sensory and/or cognitive function. Ischemic strokes~~, ~~resulting from vascular occlusion~~, ~~is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors~~.~~<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis~~ (~~RTD~~) ~~[MIM~~:[http://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-~~onset oligohydramnios (the Potter phenotype)~~.~~<ref>~~PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[http://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[http://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:~~15277638~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu~~, ~~this results in an increase~~ of the ~~vasoconstrictor activity of angiotensin~~. ~~Also able to inactivate bradykinin, a potent vasodilator~~. ~~Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[3l3n]] 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=3L3N OCA].~~	+

	==See Also==		==See Also==
-	*[[Angiotensin-Converting Enzyme\|Angiotensin-Converting Enzyme]]
	*[[Carboxypeptidase\|Carboxypeptidase]]		*[[Carboxypeptidase\|Carboxypeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020233165</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Kroger, W L.]]	+	[[Category: Kroger, W L]]
-	[[Category: Neil, H G.O.]]	+	[[Category: Neil, H G.O]]
-	[[Category: Sewell, B T.]]	+	[[Category: Sewell, B T]]
-	[[Category: Sturrock, E D.]]	+	[[Category: Sturrock, E D]]
-	[[Category: Watermeyer, J M.]]	+	[[Category: Watermeyer, J M]]
	[[Category: Carboxypeptidase]]		[[Category: Carboxypeptidase]]
	[[Category: Enzyme-inhibitor complex]]		[[Category: Enzyme-inhibitor complex]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Testis]]		[[Category: Testis]]

OCA at 05:37, 25 March 2013

OCA — Mon, 25 Mar 2013 05:37:30 GMT

←Older revision		Revision as of 05:37, 25 March 2013
Line 1:		Line 1:
-	[[Image:3l3n.png\|left\|200px]]
-
	{{STRUCTURE_3l3n\| PDB=3l3n \| SCENE= }}		{{STRUCTURE_3l3n\| PDB=3l3n \| SCENE= }}
-
	===Testis ACE co-crystal structure with novel inhibitor lisW===		===Testis ACE co-crystal structure with novel inhibitor lisW===
		+	{{ABSTRACT_PUBMED_20233165}}

-	~~{{ABSTRACT_PUBMED_20233165}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR) [MIM:[http://omim.org/entry/601367 601367]]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.<ref>PMID:15534175</ref> Defects in ACE are a cause of renal tubular dysgenesis (RTD) [MIM:[http://omim.org/entry/267430 267430]]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref> Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3) [MIM:[http://omim.org/entry/612624 612624]]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[http://omim.org/entry/614519 614519]]. A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:15277638</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ACE_HUMAN ACE_HUMAN]] Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

	==About this Structure==		==About this Structure==
Line 15:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020233165</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020233165</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Kroger, W L.]]		[[Category: Kroger, W L.]]

OCA at 09:07, 20 October 2012

OCA — Sat, 20 Oct 2012 09:07:46 GMT

←Older revision		Revision as of 09:07, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3l3n]] is a 1 chain structure ~~of [[Angiotensin-Converting Enzyme]] and [[Carboxypeptidase]]~~ 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=3L3N OCA].	+	[[3l3n]] 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=3L3N OCA].

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

OCA at 21:50, 25 July 2012

OCA — Wed, 25 Jul 2012 21:50:08 GMT

←Older revision		Revision as of 21:50, 25 July 2012
Line 1:		Line 1:
	[[Image:3l3n.png\|left\|200px]]		[[Image:3l3n.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3l3n", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3l3n\| PDB=3l3n \| SCENE= }}		{{STRUCTURE_3l3n\| PDB=3l3n \| SCENE= }}

	===Testis ACE co-crystal structure with novel inhibitor lisW===		===Testis ACE co-crystal structure with novel inhibitor lisW===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20233165}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20233165 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_20233165}}		{{ABSTRACT_PUBMED_20233165}}

OCA: Protected "3l3n" [edit=sysop:move=sysop]

OCA — Sat, 02 Jun 2012 15:23:02 GMT

Protected "3l3n" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:23, 2 June 2012