6zpq - Revision history

OCA at 11:56, 1 February 2024

OCA — Thu, 01 Feb 2024 11:56:00 GMT

←Older revision		Revision as of 11:56, 1 February 2024
Line 3:		Line 3:
	<StructureSection load='6zpq' size='340' side='right'caption='[[6zpq]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='6zpq' size='340' side='right'caption='[[6zpq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6zpq]] is a 4 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=6ZPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZPQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6zpq]] is a 4 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=6ZPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZPQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MXE:2-METHOXYETHANOL'>MXE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.85Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MXE:2-METHOXYETHANOL'>MXE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zpq OCA], [https://pdbe.org/6zpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zpq RCSB], [https://www.ebi.ac.uk/pdbsum/6zpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zpq 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=6zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zpq OCA], [https://pdbe.org/6zpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zpq RCSB], [https://www.ebi.ac.uk/pdbsum/6zpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zpq 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Acharya~~, K R~~]]	+	[[Category: Acharya KR]]
-	[[Category: Cozier~~, G E]]~~	+	[[Category: Cozier GE]]
-	~~[[Category: Angiotensin-1 converting enzyme]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metalloprotease]]~~	+
-	~~[[Category: Open conformation~~]]	+

OCA at 06:55, 14 April 2021

OCA — Wed, 14 Apr 2021 06:55:07 GMT

←Older revision		Revision as of 06:55, 14 April 2021
Line 1:		Line 1:

	==Crystal structure of the open conformation of Angiotensin-1 converting enzyme N-domain.==		==Crystal structure of the open conformation of Angiotensin-1 converting enzyme N-domain.==
-	<StructureSection load='6zpq' size='340' side='right'caption='[[6zpq]]' scene=''>	+	<StructureSection load='6zpq' size='340' side='right'caption='[[6zpq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZPQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6ZPQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6zpq]] is a 4 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=6ZPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZPQ FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zpq OCA], [~~http~~://pdbe.org/6zpq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6zpq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6zpq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6zpq ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MXE:2-METHOXYETHANOL'>MXE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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=6zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zpq OCA], [https://pdbe.org/6zpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zpq RCSB], [https://www.ebi.ac.uk/pdbsum/6zpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zpq ProSAT]</span></td></tr>
	</table>		</table>
		+	== 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>
		+	== 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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Angiotensin-1 converting enzyme (ACE) is a key enzyme in the renin-angiotensin-aldosterone and kinin systems where it cleaves angiotensin I and bradykinin peptides, respectively. However, ACE also participates in numerous other physiological functions, can hydrolyse many peptide substrates, and has various exo- and endopeptidase activities. ACE achieves this complexity by containing two homologous catalytic domains (N- and C-domains), which exhibit different substrate specificities. Here we present the first open conformation structures of ACE N-domain, and a unique closed C-domain structure (2.0 A) where the C-terminus of a symmetry-related molecule is observed inserted into the active site cavity and binding to the zinc ion. The open native N-domain structure (1.85 A) enables comparison with ACE2, a homologue previously observed in open and closed states. An open S2 _S'-mutant N-domain structure (2.80 A) includes mutated residues in the S2 - and S'- subsites that effect ligand binding, but are distal to the binding site. Analysis of these structures provides important insights into how structural features of the ACE domains are able to accommodate the wide variety of substrates and allow different peptidase activities.
		+
		+	Angiotensin-converting enzyme open for business: structural insights into the sub-domain dynamics.,Cozier GE, Lubbe L, Sturrock ED, Acharya KR FEBS J. 2020 Oct 17. doi: 10.1111/febs.15601. PMID:33067882<ref>PMID:33067882</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6zpq" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Angiotensin-Converting Enzyme 3D structures\|Angiotensin-Converting Enzyme 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Acharya KR]]	+	[[Category: Acharya, K R]]
-	[[Category: Cozier GE]]	+	[[Category: Cozier, G E]]
		+	[[Category: Angiotensin-1 converting enzyme]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metalloprotease]]
		+	[[Category: Open conformation]]

OCA at 20:35, 28 October 2020

OCA — Wed, 28 Oct 2020 20:35:35 GMT

←Older revision		Revision as of 20:35, 28 October 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 6zpq is ON HOLD until Paper Publication~~	+	==Crystal structure of the open conformation of Angiotensin-1 converting enzyme N-domain.==
-		+	<StructureSection load='6zpq' size='340' side='right'caption='[[6zpq]]' scene=''>
-	~~Authors: Cozier, G.E., Acharya, K.R.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZPQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZPQ FirstGlance]. <br>
-	~~Description:~~ Crystal structure of the open conformation of Angiotensin-1 converting enzyme N-domain.	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zpq OCA], [http://pdbe.org/6zpq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zpq RCSB], [http://www.ebi.ac.uk/pdbsum/6zpq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zpq ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Acharya~~, K.R~~]]	+	__TOC__
-	[[Category: Cozier~~, G.E~~]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Acharya KR]]
		+	[[Category: Cozier GE]]

OCA: Protected "6zpq" [edit=sysop:move=sysop]

OCA — Wed, 22 Jul 2020 08:10:57 GMT

Protected "6zpq" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:10, 22 July 2020

OCA: New page: '''Unreleased structure''' The entry 6zpq is ON HOLD until Paper Publication Authors: Cozier, G.E., Acharya, K.R. Description: Crystal structure of the open conformation of Angiotensin...

OCA — Wed, 22 Jul 2020 08:10:55 GMT

New page: '''Unreleased structure''' The entry 6zpq is ON HOLD until Paper Publication Authors: Cozier, G.E., Acharya, K.R. Description: Crystal structure of the open conformation of Angiotensin...

New page

'''Unreleased structure'''

The entry 6zpq is ON HOLD until Paper Publication

Authors: Cozier, G.E., Acharya, K.R.

Description: Crystal structure of the open conformation of Angiotensin-1 converting enzyme N-domain.
[[Category: Unreleased Structures]]
[[Category: Acharya, K.R]]
[[Category: Cozier, G.E]]