1aw0 - Revision history

OCA at 15:28, 13 March 2024

OCA — Wed, 13 Mar 2024 15:28:51 GMT

←Older revision		Revision as of 15:28, 13 March 2024
Line 1:		Line 1:

	==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==		==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==
-	<StructureSection load='1aw0' size='340' side='right'caption='[[1aw0~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1aw0' size='340' side='right'caption='[[1aw0]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~='plainlinks'>[https://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [https://pdbe.org/1aw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw0 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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [https://pdbe.org/1aw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw0 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[https://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[https://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[https://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>	+	[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[https://omim.org/entry/309400 309400]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[https://omim.org/entry/304150 304150]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[https://omim.org/entry/300489 300489]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.	+	[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 21:
	</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=1aw0 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=1aw0 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(I)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like beta alpha beta beta alpha beta fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(I)-bound structure. Ag(I) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(I) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif.
-
-	Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.,Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ Nat Struct Biol. 1998 Jan;5(1):47-54. PMID:9437429<ref>PMID:9437429</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1aw0" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Hydrogen/potassium-exchanging ATPase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fairbrother~~, W J~~]]	+	[[Category: Fairbrother WJ]]
-	[[Category: Gitschier, J]]	+	[[Category: Gitschier J]]
-	~~[[Category: Copper-binding domain]]~~	+
-	~~[[Category: Copper-transporting atpase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 10:27, 14 July 2021

OCA — Wed, 14 Jul 2021 10:27:05 GMT

←Older revision		Revision as of 10:27, 14 July 2021
Line 3:		Line 3:
	<StructureSection load='1aw0' size='340' side='right'caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1aw0' size='340' side='right'caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [~~http~~://pdbe.org/1aw0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1aw0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw0 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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [https://pdbe.org/1aw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw0 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[~~http~~://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[~~http~~://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[~~http~~://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>	+	[[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[https://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[https://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[https://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.	+	[[https://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:06, 10 October 2019

OCA — Thu, 10 Oct 2019 07:06:35 GMT

←Older revision		Revision as of 07:06, 10 October 2019
Line 1:		Line 1:

	==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==		==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==
-	<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1aw0' size='340' side='right'caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw0_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw0_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1aw0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1aw0" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase 3D structures\|ATPase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	[[Category: Human]]		[[Category: Human]]
	[[Category: Hydrogen/potassium-exchanging ATPase]]		[[Category: Hydrogen/potassium-exchanging ATPase]]
		+	[[Category: Large Structures]]
	[[Category: Fairbrother, W J]]		[[Category: Fairbrother, W J]]
	[[Category: Gitschier, J]]		[[Category: Gitschier, J]]

OCA at 10:43, 8 November 2017

OCA — Wed, 08 Nov 2017 10:43:23 GMT

←Older revision		Revision as of 10:43, 8 November 2017
Line 1:		Line 1:
		+
	==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==		==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==
	<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://pdbe.org/1aw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://pdbe.org/1aw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw0 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1aw0" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1aw0" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:06, 7 February 2016

OCA — Sun, 07 Feb 2016 17:06:12 GMT

←Older revision		Revision as of 17:06, 7 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=1aw0 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 03:29, 10 September 2015

OCA — Thu, 10 Sep 2015 03:29:32 GMT

←Older revision		Revision as of 03:29, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://pdbe.org/1aw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 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 1aw0" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hydrogen/potassium-exchanging ATPase]]		[[Category: Hydrogen/potassium-exchanging ATPase]]
	[[Category: Fairbrother, W J]]		[[Category: Fairbrother, W J]]

OCA at 11:51, 22 December 2014

OCA — Mon, 22 Dec 2014 11:51:01 GMT

←Older revision		Revision as of 11:51, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[http://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[http://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[http://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>		[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[http://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[http://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[http://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>
Line 37:		Line 37:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hydrogen/potassium-exchanging ATPase]]		[[Category: Hydrogen/potassium-exchanging ATPase]]
-	[[Category: Fairbrother, W J.]]	+	[[Category: Fairbrother, W J]]
-	[[Category: Gitschier, J.]]	+	[[Category: Gitschier, J]]
	[[Category: Copper-binding domain]]		[[Category: Copper-binding domain]]
	[[Category: Copper-transporting atpase]]		[[Category: Copper-transporting atpase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 17:29, 29 September 2014

OCA — Mon, 29 Sep 2014 17:29:14 GMT

←Older revision		Revision as of 17:29, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1aw0\| PDB=1aw0 \| SCENE= }}~~	+	==FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES==
-	===FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES===	+	<StructureSection load='1aw0' size='340' side='right' caption='[[1aw0]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_9437429}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW0 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen/potassium-exchanging_ATPase Hydrogen/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.10 3.6.3.10] </span></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=1aw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aw0 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw0 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[http://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref> <ref>PMID:7977350</ref> <ref>PMID:8981948</ref> <ref>PMID:10401004</ref> <ref>PMID:10319589</ref> <ref>PMID:11241493</ref> <ref>PMID:11350187</ref> <ref>PMID:15981243</ref> <ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[http://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref> <ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[http://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.
		+	== 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/aw/1aw0_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 ==
		+	Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(I)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like beta alpha beta beta alpha beta fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(I)-bound structure. Ag(I) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(I) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif.

-	~~==Disease==~~	+	Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.,Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ Nat Struct Biol. 1998 Jan;5(1):47-54. PMID:9437429<ref>PMID:9437429</ref>
-	~~[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are~~ the ~~cause of~~ Menkes ~~disease (MNKD) [MIM:[http://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X~~-~~linked recessive disorder of copper metabolism characterized by generalized copper deficiency~~. ~~MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration~~, ~~early growth retardation~~, ~~peculiar hair~~, ~~hypopigmentation~~, ~~cutis laxa~~, ~~vascular complications and death in early childhood~~. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref><ref>PMID:7977350</ref><ref>PMID:8981948</ref><ref>PMID:10401004</ref><ref>PMID:10319589</ref><ref>PMID:11241493</ref><ref>PMID:11350187</ref><ref>PMID:15981243</ref><ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (~~OHS~~) ~~[MIM~~:~~[http://omim.org/entry/304150 304150]]; also known as X~~-~~linked cutis laxa~~. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref><ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[http://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:~~20170900~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway~~, ~~when localized in~~ the ~~trans-Golgi network~~. ~~Under conditions~~ of ~~elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1aw0]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA].~~	+

	==See Also==		==See Also==
	*[[ATPase\|ATPase]]		*[[ATPase\|ATPase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:009437429</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hydrogen/potassium-exchanging ATPase]]		[[Category: Hydrogen/potassium-exchanging ATPase]]

OCA at 22:10, 24 March 2013

OCA — Sun, 24 Mar 2013 22:10:32 GMT

←Older revision		Revision as of 22:10, 24 March 2013
Line 1:		Line 1:
-	[[Image:1aw0.png\|left\|200px]]
-
	{{STRUCTURE_1aw0\| PDB=1aw0 \| SCENE= }}		{{STRUCTURE_1aw0\| PDB=1aw0 \| SCENE= }}
-
	===FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES===		===FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES===
		+	{{ABSTRACT_PUBMED_9437429}}

-	~~{{ABSTRACT_PUBMED_9437429}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] Defects in ATP7A are the cause of Menkes disease (MNKD) [MIM:[http://omim.org/entry/309400 309400]]; also known as kinky hair disease. MNKD is an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency. MNKD results in progressive neurodegeneration and connective-tissue disturbances: focal cerebral and cerebellar degeneration, early growth retardation, peculiar hair, hypopigmentation, cutis laxa, vascular complications and death in early childhood. The clinical features result from the dysfunction of several copper-dependent enzymes.<ref>PMID:10079817</ref><ref>PMID:7977350</ref><ref>PMID:8981948</ref><ref>PMID:10401004</ref><ref>PMID:10319589</ref><ref>PMID:11241493</ref><ref>PMID:11350187</ref><ref>PMID:15981243</ref><ref>PMID:22992316</ref> Defects in ATP7A are the cause of occipital horn syndrome (OHS) [MIM:[http://omim.org/entry/304150 304150]]; also known as X-linked cutis laxa. OHS is an X-linked recessive disorder of copper metabolism. Common features are unusual facial appearance, skeletal abnormalities, chronic diarrhea and genitourinary defects. The skeletal abnormalities included occipital horns, short, broad clavicles, deformed radii, ulnae and humeri, narrowing of the rib cage, undercalcified long bones with thin cortical walls and coxa valga.<ref>PMID:9246006</ref><ref>PMID:17108763</ref> Defects in ATP7A are a cause of distal spinal muscular atrophy X-linked type 3 (DSMAX3) [MIM:[http://omim.org/entry/300489 300489]]. DSMAX3 is a neuromuscular disorder. Distal spinal muscular atrophy, also known as distal hereditary motor neuronopathy, represents a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.<ref>PMID:20170900</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ATP7A_HUMAN ATP7A_HUMAN]] May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:009437429</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009437429</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hydrogen/potassium-exchanging ATPase]]		[[Category: Hydrogen/potassium-exchanging ATPase]]

OCA at 07:19, 20 October 2012

OCA — Sat, 20 Oct 2012 07:19:08 GMT

←Older revision		Revision as of 07:19, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1aw0]] is a 1 chain structure ~~of [[ATPase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA].	+	[[1aw0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW0 OCA].

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