3cz9 - Revision history

OCA at 12:35, 30 August 2023

2023-08-30T12:35:35Z

←Older revision		Revision as of 12:35, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='3cz9' size='340' side='right'caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>		<StructureSection load='3cz9' size='340' side='right'caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=P4C:O~~-~~ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</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]] 1.15Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]~~</~~div~~>~~</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PARK7 ([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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [https://pdbe.org/3cz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3cz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cz9 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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [https://pdbe.org/3cz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3cz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cz9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[https://omim.org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>	+	[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[https://omim.org/entry/606324 606324]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>	+	[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>
	== 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: Hasim, S]]	+	[[Category: Hasim S]]
-	[[Category: Lakshminarasimhan, M]]	+	[[Category: Lakshminarasimhan M]]
-	[[Category: Pozharski, E]]	+	[[Category: Pozharski E]]
-	[[Category: Remington~~, B C~~]]	+	[[Category: Remington BC]]
-	[[Category: Wilson~~, M A~~]]	+	[[Category: Wilson MA]]
-	[[Category: Witt~~, A C]]~~	+	[[Category: Witt AC]]
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Oncogene]]~~	+
-	~~[[Category: Oxidation]]~~	+
-	~~[[Category: Parkinson disease]]~~	+
-	~~[[Category: Reactive cysteine]]~~	+
-	~~[[Category: Unknown function~~]]	+

OCA at 19:16, 20 October 2021

2021-10-20T19:16:56Z

←Older revision		Revision as of 19:16, 20 October 2021
Line 1:		Line 1:

	==Crystal Structure of E18L DJ-1==		==Crystal Structure of E18L DJ-1==
-	<StructureSection load='3cz9' size='340' side='right' caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>	+	<StructureSection load='3cz9' size='340' side='right'caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PARK7 ([~~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">PARK7 ([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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [~~http~~://pdbe.org/3cz9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3cz9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3cz9 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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [https://pdbe.org/3cz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3cz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cz9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[~~http~~://omim.org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>	+	[[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[https://omim.org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>	+	[[https://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3cz9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3cz9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Protein DJ-1\|Protein DJ-1]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hasim, S]]		[[Category: Hasim, S]]
	[[Category: Lakshminarasimhan, M]]		[[Category: Lakshminarasimhan, M]]

OCA at 13:44, 7 November 2018

2018-11-07T13:44:27Z

←Older revision		Revision as of 13:44, 7 November 2018
Line 17:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/3cz9_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/3cz9_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 44:		Line 44:
	[[Category: Witt, A C]]		[[Category: Witt, A C]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
		+	[[Category: Cytoplasm]]
	[[Category: Nucleus]]		[[Category: Nucleus]]
	[[Category: Oncogene]]		[[Category: Oncogene]]

OCA at 17:38, 5 August 2016

2016-08-05T17:38:31Z

←Older revision		Revision as of 17:38, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of E18L DJ-1==		==Crystal Structure of E18L DJ-1==
	<StructureSection load='3cz9' size='340' side='right' caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>		<StructureSection load='3cz9' size='340' side='right' caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PARK7 ([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">PARK7 ([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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cz9 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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [http://pdbe.org/3cz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cz9 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=3cz9 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 3cz9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hasim, S]]		[[Category: Hasim, S]]
	[[Category: Lakshminarasimhan, M]]		[[Category: Lakshminarasimhan, M]]

OCA at 13:58, 18 December 2014

2014-12-18T13:58:05Z

←Older revision		Revision as of 13:58, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3cz9~~\| ~~PDB~~=3cz9 \| ~~SCENE~~= }}	+	==Crystal Structure of E18L DJ-1==
-	===~~Crystal Structure~~ of ~~E18L DJ~~-1===	+	<StructureSection load='3cz9' size='340' side='right' caption='[[3cz9]], [[Resolution\|resolution]] 1.15Å' scene=''>
-	~~{{ABSTRACT_PUBMED_18570440}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3cz9]] 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=3CZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CZ9 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2or3\|2or3]], [[3cy6\|3cy6]], [[3cyf\|3cyf]], [[1p5f\|1p5f]], [[3cza\|3cza]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PARK7 ([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=3cz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cz9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cz9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cz9 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[http://omim.org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref> <ref>PMID:12446870</ref> <ref>PMID:14713311</ref> <ref>PMID:12953260</ref> <ref>PMID:15365989</ref> <ref>PMID:14607841</ref> <ref>PMID:15254937</ref> <ref>PMID:17846173</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref> <ref>PMID:11477070</ref> <ref>PMID:12612053</ref> <ref>PMID:14749723</ref> <ref>PMID:15502874</ref> <ref>PMID:15976810</ref> <ref>PMID:16390825</ref> <ref>PMID:17015834</ref> <ref>PMID:18626009</ref> <ref>PMID:18711745</ref> <ref>PMID:20304780</ref> <ref>PMID:21097510</ref> <ref>PMID:12939276</ref> <ref>PMID:15181200</ref>
		+	== 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/cz/3cz9_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 DJ-1, a disease-associated protein that protects cells from oxidative stress, contains an oxidation-sensitive cysteine (C106) that is essential for its cytoprotective activity. The origin of C106 reactivity is obscure, due in part to the absence of an experimentally determined p K a value for this residue. We have used atomic-resolution X-ray crystallography and UV spectroscopy to show that C106 has a depressed p K a of 5.4 +/- 0.1 and that the C106 thiolate accepts a hydrogen bond from a protonated glutamic acid side chain (E18). X-ray crystal structures and cysteine p K a analysis of several site-directed substitutions at residue 18 demonstrate that the protonated carboxylic acid side chain of E18 is required for the maximal stabilization of the C106 thiolate. A nearby arginine residue (R48) participates in a guanidinium stacking interaction with R28 from the other monomer in the DJ-1 dimer and elevates the p K a of C106 by binding an anion that electrostatically suppresses thiol ionization. Our results show that the ionizable residues (E18, R48, and R28) surrounding C106 affect its p K a in a way that is contrary to expectations based on the typical ionization behavior of glutamic acid and arginine. Lastly, a search of the Protein Data Bank (PDB) produces several candidate hydrogen-bonded aspartic/glutamic acid-cysteine interactions, which we propose are particularly common in the DJ-1 superfamily.

-	~~==Disease==~~	+	Cysteine pKa depression by a protonated glutamic acid in human DJ-1.,Witt AC, Lakshminarasimhan M, Remington BC, Hasim S, Pozharski E, Wilson MA Biochemistry. 2008 Jul 15;47(28):7430-40. Epub 2008 Jun 21. PMID:18570440<ref>PMID:18570440</ref>
-	~~[[http://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects~~ in ~~PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[http://omim~~.~~org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor~~, ~~postural tremor~~, ~~bradykinesia~~, ~~muscular rigidity~~, ~~anxiety and psychotic episodes. PARK7 has onset before 40 years~~, ~~slow progression and initial good response to levodopa~~. ~~Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex~~ (~~Guam disease~~).~~<ref>~~PMID:~~12851414</ref><ref>PMID:12446870</ref><ref>PMID:14713311</ref><ref>PMID:12953260</ref><ref>PMID:15365989</ref><ref>PMID:14607841</ref><ref>PMID:15254937</ref>~~<ref>PMID:~~17846173~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays~~ a ~~role in regulating expression or stability~~ of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. ~~Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death~~. ~~May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal~~ of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<~~ref~~>~~PMID:9070310~~</~~ref~~><ref>PMID:11477070</ref><ref>PMID:12612053</ref><ref>PMID:14749723</ref><ref>PMID:15502874</ref><ref>PMID:15976810</ref><ref>PMID:16390825</ref><ref>PMID:17015834</ref><ref>PMID:18626009</ref><ref>PMID:18711745</ref><ref>PMID:20304780</ref><ref>PMID:21097510</ref><ref>PMID:12939276</ref><ref>PMID:15181200</ref>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[3cz9]] 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=3CZ9 OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:018570440</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hasim, S.]]	+	[[Category: Hasim, S]]
-	[[Category: Lakshminarasimhan, M.]]	+	[[Category: Lakshminarasimhan, M]]
-	[[Category: Pozharski, E.]]	+	[[Category: Pozharski, E]]
-	[[Category: Remington, B C.]]	+	[[Category: Remington, B C]]
-	[[Category: Wilson, M A.]]	+	[[Category: Wilson, M A]]
-	[[Category: Witt, A C.]]	+	[[Category: Witt, A C]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Nucleus]]		[[Category: Nucleus]]

OCA at 02:39, 25 March 2013

2013-03-25T02:39:25Z

←Older revision		Revision as of 02:39, 25 March 2013
Line 1:		Line 1:
-	[[Image:3cz9.png\|left\|200px]]
-
	{{STRUCTURE_3cz9\| PDB=3cz9 \| SCENE= }}		{{STRUCTURE_3cz9\| PDB=3cz9 \| SCENE= }}
-
	===Crystal Structure of E18L DJ-1===		===Crystal Structure of E18L DJ-1===
		+	{{ABSTRACT_PUBMED_18570440}}

-	~~{{ABSTRACT_PUBMED_18570440}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Defects in PARK7 are the cause of Parkinson disease type 7 (PARK7) [MIM:[http://omim.org/entry/606324 606324]]. A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).<ref>PMID:12851414</ref><ref>PMID:12446870</ref><ref>PMID:14713311</ref><ref>PMID:12953260</ref><ref>PMID:15365989</ref><ref>PMID:14607841</ref><ref>PMID:15254937</ref><ref>PMID:17846173</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/PARK7_HUMAN PARK7_HUMAN]] Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone.<ref>PMID:9070310</ref><ref>PMID:11477070</ref><ref>PMID:12612053</ref><ref>PMID:14749723</ref><ref>PMID:15502874</ref><ref>PMID:15976810</ref><ref>PMID:16390825</ref><ref>PMID:17015834</ref><ref>PMID:18626009</ref><ref>PMID:18711745</ref><ref>PMID:20304780</ref><ref>PMID:21097510</ref><ref>PMID:12939276</ref><ref>PMID:15181200</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018570440</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018570440</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hasim, S.]]		[[Category: Hasim, S.]]

OCA: Protected "3cz9" [edit=sysop:move=sysop]

2013-01-07T20:15:57Z

Protected "3cz9" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:15, 7 January 2013

OCA at 20:15, 7 January 2013

2013-01-07T20:15:56Z

←Older revision		Revision as of 20:15, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3cz9.png\|left\|200px]]		[[Image:3cz9.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3cz9", 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_3cz9\| PDB=3cz9 \| SCENE= }}		{{STRUCTURE_3cz9\| PDB=3cz9 \| SCENE= }}

	===Crystal Structure of E18L DJ-1===		===Crystal Structure of E18L DJ-1===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18570440}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18570440 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18570440}}		{{ABSTRACT_PUBMED_18570440}}
-
-	==Disease==
-	Known disease associated with this structure: Amyotrophic lateral sclerosis-Parkinsonism/dementia complex 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602533 602533]], Parkinson disease 7, autosomal recessive early-onset OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602533 602533]]

	==About this Structure==		==About this Structure==
-	~~3CZ9~~ is a 1 chain structure of 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=3CZ9 OCA].	+	[[3cz9]] 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=3CZ9 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18570440~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018570440</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hasim, S.]]		[[Category: Hasim, S.]]
Line 35:		Line 20:
	[[Category: Witt, A C.]]		[[Category: Witt, A C.]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
-	[[Category: Cytoplasm]]
	[[Category: Nucleus]]		[[Category: Nucleus]]
	[[Category: Oncogene]]		[[Category: Oncogene]]
Line 42:		Line 26:
	[[Category: Reactive cysteine]]		[[Category: Reactive cysteine]]
	[[Category: Unknown function]]		[[Category: Unknown function]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:37:08 2009''

OCA at 04:37, 18 February 2009

2009-02-18T04:37:09Z

←Older revision		Revision as of 04:37, 18 February 2009
Line 23:		Line 23:

	==About this Structure==		==About this Structure==
-	3CZ9 is a ~~[[Single protein]]~~ structure of 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=3CZ9 OCA].	+	3CZ9 is a 1 chain structure of 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=3CZ9 OCA].

	==Reference==		==Reference==
-	Cysteine pKa depression by a protonated glutamic acid in human DJ-1., Witt AC, Lakshminarasimhan M, Remington BC, Hasim S, Pozharski E, Wilson MA, Biochemistry. 2008 Jul 15;47(28):7430-40. Epub 2008 Jun 21. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18570440 18570440]~~	+	<ref group="xtra">PMID:18570440</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Hasim, S.]]		[[Category: Hasim, S.]]
	[[Category: Lakshminarasimhan, M.]]		[[Category: Lakshminarasimhan, M.]]
Line 44:		Line 43:
	[[Category: Unknown function]]		[[Category: Unknown function]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jul 9 10~~:11:~~35 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:37:08 2009''

OCA at 07:11, 9 July 2008

2008-07-09T07:11:35Z

←Older revision		Revision as of 07:11, 9 July 2008
Line 1:		Line 1:
	{{Seed}}		{{Seed}}
-	[[Image:3cz9.~~jpg~~\|left\|200px]]	+	[[Image:3cz9.png\|left\|200px]]

	<!--		<!--
Line 12:		Line 12:
	===Crystal Structure of E18L DJ-1===		===Crystal Structure of E18L DJ-1===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18570440}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18570440 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18570440}}

	==Disease==		==Disease==
Line 18:		Line 24:
	==About this Structure==		==About this Structure==
	3CZ9 is a [[Single protein]] structure of 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=3CZ9 OCA].		3CZ9 is a [[Single protein]] structure of 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=3CZ9 OCA].
		+
		+	==Reference==
		+	Cysteine pKa depression by a protonated glutamic acid in human DJ-1., Witt AC, Lakshminarasimhan M, Remington BC, Hasim S, Pozharski E, Wilson MA, Biochemistry. 2008 Jul 15;47(28):7430-40. Epub 2008 Jun 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18570440 18570440]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Single protein]]		[[Category: Single protein]]
Line 35:		Line 44:
	[[Category: Unknown function]]		[[Category: Unknown function]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Jul ~~3 11~~:31:07 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 9 10:11:35 2008''