3hqr - Revision history

OCA at 15:52, 1 November 2023

OCA — Wed, 01 Nov 2023 15:52:57 GMT

←Older revision		Revision as of 15:52, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3hqr' size='340' side='right'caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3hqr' size='340' side='right'caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQR FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>~~, ~~<scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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]] 2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3hqu\|3hqu]], [[2g1m\|2g1m]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">PHD2 ([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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [https://pdbe.org/3hqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [https://www.ebi.ac.uk/pdbsum/3hqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqr 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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [https://pdbe.org/3hqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [https://www.ebi.ac.uk/pdbsum/3hqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqr ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[https://omim.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref> <ref>PMID:17579185</ref>	+	[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[https://omim.org/entry/609820 609820]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref> <ref>PMID:17579185</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref> <ref>PMID:12351678</ref> <ref>PMID:15897452</ref> <ref>PMID:19339211</ref> <ref>PMID:21792862</ref> [[https://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref> <ref>PMID:11566883</ref> <ref>PMID:11292861</ref> <ref>PMID:15465032</ref> <ref>PMID:16543236</ref> <ref>PMID:16973622</ref> <ref>PMID:17610843</ref> <ref>PMID:19528298</ref> <ref>PMID:20624928</ref>	+	[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref> <ref>PMID:12351678</ref> <ref>PMID:15897452</ref> <ref>PMID:19339211</ref> <ref>PMID:21792862</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 34:
	==See Also==		==See Also==
	*[[Factor inhibiting HIF\|Factor inhibiting HIF]]		*[[Factor inhibiting HIF\|Factor inhibiting HIF]]
-	*[[~~Prolyl~~ hydroxylase domain\|~~Prolyl~~ hydroxylase domain]]	+	*[[Polyl hydroxylase domain 3D structures\|Polyl hydroxylase domain 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chowdhury, R]]	+	[[Category: Chowdhury R]]
-	[[Category: McDonough~~, M A~~]]	+	[[Category: McDonough MA]]
-	[[Category: Schofield~~, C J]]~~	+	[[Category: Schofield CJ]]
-	~~[[Category: Activator]]~~	+
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Congenital erythrocytosis]]~~	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Disease mutation]]~~	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Double stranded beta-helix]]~~	+
-	~~[[Category: Hydroxylation]]~~	+
-	~~[[Category: Iron]]~~	+
-	~~[[Category: Isopeptide bond]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase-transcription complex]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: S-nitrosylation]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation]]~~	+
-	~~[[Category: Ubl conjugation]]~~	+
-	~~[[Category: Vitamin c]]~~	+
-	~~[[Category: Zinc]]~~	+
-	~~[[Category: Zinc-finger~~]]	+

OCA at 07:45, 10 November 2021

OCA — Wed, 10 Nov 2021 07:45:01 GMT

←Older revision		Revision as of 07:45, 10 November 2021
Line 1:		Line 1:

	==PHD2:Mn:NOG:HIF1-alpha substrate complex==		==PHD2:Mn:NOG:HIF1-alpha substrate complex==
-	<StructureSection load='3hqr' size='340' side='right' caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='3hqr' size='340' side='right'caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQR FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hqu\|3hqu]], [[2g1m\|2g1m]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hqu\|3hqu]], [[2g1m\|2g1m]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PHD2 ([~~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">PHD2 ([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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [~~http~~://pdbe.org/3hqr PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hqr PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqr 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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [https://pdbe.org/3hqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [https://www.ebi.ac.uk/pdbsum/3hqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqr ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[~~http~~://omim.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref> <ref>PMID:17579185</ref>	+	[[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[https://omim.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref> <ref>PMID:17579185</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref> <ref>PMID:12351678</ref> <ref>PMID:15897452</ref> <ref>PMID:19339211</ref> <ref>PMID:21792862</ref> [[~~http~~://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref> <ref>PMID:11566883</ref> <ref>PMID:11292861</ref> <ref>PMID:15465032</ref> <ref>PMID:16543236</ref> <ref>PMID:16973622</ref> <ref>PMID:17610843</ref> <ref>PMID:19528298</ref> <ref>PMID:20624928</ref>	+	[[https://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref> <ref>PMID:12351678</ref> <ref>PMID:15897452</ref> <ref>PMID:19339211</ref> <ref>PMID:21792862</ref> [[https://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref> <ref>PMID:11566883</ref> <ref>PMID:11292861</ref> <ref>PMID:15465032</ref> <ref>PMID:16543236</ref> <ref>PMID:16973622</ref> <ref>PMID:17610843</ref> <ref>PMID:19528298</ref> <ref>PMID:20624928</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/3hqr_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/3hqr_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 34:		Line 34:

	==See Also==		==See Also==
-	*[[~~Molecular Playground/~~Prolyl ~~Hydroxylase Domain (PHD) Enzyme~~\|~~Molecular Playground/~~Prolyl ~~Hydroxylase Domain (PHD) Enzyme~~]]	+	*[[Factor inhibiting HIF\|Factor inhibiting HIF]]
		+	*[[Prolyl hydroxylase domain\|Prolyl hydroxylase domain]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 41:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Chowdhury, R]]		[[Category: Chowdhury, R]]
	[[Category: McDonough, M A]]		[[Category: McDonough, M A]]

OCA at 07:44, 1 November 2017

OCA — Wed, 01 Nov 2017 07:44:29 GMT

←Older revision		Revision as of 07:44, 1 November 2017
Line 1:		Line 1:
		+
	==PHD2:Mn:NOG:HIF1-alpha substrate complex==		==PHD2:Mn:NOG:HIF1-alpha substrate complex==
	<StructureSection load='3hqr' size='340' side='right' caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3hqr' size='340' side='right' caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HQR FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HQR FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hqu\|3hqu]], [[2g1m\|2g1m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hqu\|3hqu]], [[2g1m\|2g1m]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PHD2 ([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">PHD2 ([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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [http://www.ebi.ac.uk/pdbsum/3hqr 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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [http://pdbe.org/3hqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [http://www.ebi.ac.uk/pdbsum/3hqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqr 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=3hqr 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 3hqr" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[~~Factor inhibiting HIF\|Factor inhibiting HIF]]~~	+	*[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme\|Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]
-	*[[Hypoxia-inducible factor prolyl hydroxylase\|Hypoxia-inducible factor prolyl hydroxylase]]	+
-	*[[Prolyl ~~hydroxylase domain~~\|Prolyl ~~hydroxylase domain~~]]	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chowdhury, R]]		[[Category: Chowdhury, R]]
	[[Category: McDonough, M A]]		[[Category: McDonough, M A]]
	[[Category: Schofield, C J]]		[[Category: Schofield, C J]]
	[[Category: Activator]]		[[Category: Activator]]
		+	[[Category: Alternative splicing]]
	[[Category: Congenital erythrocytosis]]		[[Category: Congenital erythrocytosis]]
		+	[[Category: Cytoplasm]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
Line 57:		Line 59:
	[[Category: Oxidoreductase-transcription complex]]		[[Category: Oxidoreductase-transcription complex]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
	[[Category: S-nitrosylation]]		[[Category: S-nitrosylation]]
	[[Category: Transcription]]		[[Category: Transcription]]
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
		+	[[Category: Ubl conjugation]]
	[[Category: Vitamin c]]		[[Category: Vitamin c]]
		+	[[Category: Zinc]]
	[[Category: Zinc-finger]]		[[Category: Zinc-finger]]

OCA at 14:54, 18 December 2014

OCA — Thu, 18 Dec 2014 14:54:36 GMT

←Older revision		Revision as of 14:54, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3hqr~~\| ~~PDB~~=3hqr \| ~~SCENE~~= }}	+	==PHD2:Mn:NOG:HIF1-alpha substrate complex==
-	===PHD2:Mn:~~NOG~~:~~HIF1~~-alpha ~~substrate~~ complex===	+	<StructureSection load='3hqr' size='340' side='right' caption='[[3hqr]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19604478}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3hqr]] is a 2 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=3HQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HQR FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3hqu\|3hqu]], [[2g1m\|2g1m]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PHD2 ([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=3hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hqr RCSB], [http://www.ebi.ac.uk/pdbsum/3hqr PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[http://omim.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref> <ref>PMID:17579185</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref> <ref>PMID:12351678</ref> <ref>PMID:15897452</ref> <ref>PMID:19339211</ref> <ref>PMID:21792862</ref> [[http://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref> <ref>PMID:11566883</ref> <ref>PMID:11292861</ref> <ref>PMID:15465032</ref> <ref>PMID:16543236</ref> <ref>PMID:16973622</ref> <ref>PMID:17610843</ref> <ref>PMID:19528298</ref> <ref>PMID:20624928</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/hq/3hqr_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 ==
		+	The oxygen-dependent hydroxylation of proline residues in the alpha subunit of hypoxia-inducible transcription factor (HIFalpha) is central to the hypoxic response in animals. Prolyl hydroxylation of HIFalpha increases its binding to the von Hippel-Lindau protein (pVHL), so signaling for degradation via the ubiquitin-proteasome system. The HIF prolyl hydroxylases (PHDs, prolyl hydroxylase domain enzymes) are related to the collagen prolyl hydroxylases, but form unusually stable complexes with their Fe(II) cofactor and 2-oxoglutarate cosubstrate. We report crystal structures of the catalytic domain of PHD2, the most important of the human PHDs, in complex with the C-terminal oxygen-dependent degradation domain of HIF-1alpha. Together with biochemical analyses, the results reveal that PHD catalysis involves a mobile region that isolates the hydroxylation site and stabilizes the PHD2.Fe(II).2OG complex. The results will be of use in the design of PHD inhibitors aimed at treating anemia and ischemic disease.

-	~~==Disease==~~	+	Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases.,Chowdhury R, McDonough MA, Mecinovic J, Loenarz C, Flashman E, Hewitson KS, Domene C, Schofield CJ Structure. 2009 Jul 15;17(7):981-9. PMID:19604478<ref>PMID:19604478</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3~~ (~~ECYT3~~) ~~[MIM~~:~~[http://omim~~.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:~~16407130</ref>~~<ref>PMID:~~17579185~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http://www.uniprot.org/uniprot~~/~~EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes~~, ~~under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates~~ a ~~specific proline found in each~~ of the ~~oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A~~. ~~Also hydroxylates HIF2A~~. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<~~ref~~>~~PMID:11595184~~</~~ref~~><ref>PMID:12351678</ref><ref>PMID:15897452</ref><ref>PMID:19339211</ref><ref>PMID:21792862</ref> [[http://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref><ref>PMID:11566883</ref><ref>PMID:11292861</ref><ref>PMID:15465032</ref><ref>PMID:16543236</ref><ref>PMID:16973622</ref><ref>PMID:17610843</ref><ref>PMID:19528298</ref><ref>PMID:20624928</ref>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3hqr]] is a 2 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=3HQR OCA].	+

	==See Also==		==See Also==
Line 16:		Line 35:
	*[[Hypoxia-inducible factor prolyl hydroxylase\|Hypoxia-inducible factor prolyl hydroxylase]]		*[[Hypoxia-inducible factor prolyl hydroxylase\|Hypoxia-inducible factor prolyl hydroxylase]]
	*[[Prolyl hydroxylase domain\|Prolyl hydroxylase domain]]		*[[Prolyl hydroxylase domain\|Prolyl hydroxylase domain]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019604478</ref><ref group="xtra">PMID:016782814</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chowdhury, R.]]	+	[[Category: Chowdhury, R]]
-	[[Category: McDonough, M A.]]	+	[[Category: McDonough, M A]]
-	[[Category: Schofield, C J.]]	+	[[Category: Schofield, C J]]
	[[Category: Activator]]		[[Category: Activator]]
	[[Category: Congenital erythrocytosis]]		[[Category: Congenital erythrocytosis]]

OCA at 18:18, 24 March 2013

OCA — Sun, 24 Mar 2013 18:18:06 GMT

←Older revision		Revision as of 18:18, 24 March 2013
Line 1:		Line 1:
-	[[Image:3hqr.png\|left\|200px]]
-
	{{STRUCTURE_3hqr\| PDB=3hqr \| SCENE= }}		{{STRUCTURE_3hqr\| PDB=3hqr \| SCENE= }}
-
	===PHD2:Mn:NOG:HIF1-alpha substrate complex===		===PHD2:Mn:NOG:HIF1-alpha substrate complex===
		+	{{ABSTRACT_PUBMED_19604478}}

-	~~{{ABSTRACT_PUBMED_19604478}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Defects in EGLN1 are the cause of familial erythrocytosis type 3 (ECYT3) [MIM:[http://omim.org/entry/609820 609820]]. ECYT3 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.<ref>PMID:16407130</ref><ref>PMID:17579185</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/EGLN1_HUMAN EGLN1_HUMAN]] Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality.<ref>PMID:11595184</ref><ref>PMID:12351678</ref><ref>PMID:15897452</ref><ref>PMID:19339211</ref><ref>PMID:21792862</ref> [[http://www.uniprot.org/uniprot/HIF1A_HUMAN HIF1A_HUMAN]] Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.<ref>PMID:9887100</ref><ref>PMID:11566883</ref><ref>PMID:11292861</ref><ref>PMID:15465032</ref><ref>PMID:16543236</ref><ref>PMID:16973622</ref><ref>PMID:17610843</ref><ref>PMID:19528298</ref><ref>PMID:20624928</ref>

	==About this Structure==		==About this Structure==
Line 16:		Line 18:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019604478</ref><ref group="xtra">PMID:016782814</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019604478</ref><ref group="xtra">PMID:016782814</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chowdhury, R.]]		[[Category: Chowdhury, R.]]

OCA at 19:17, 20 October 2012

OCA — Sat, 20 Oct 2012 19:17:12 GMT

←Older revision		Revision as of 19:17, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3hqr]] is a 2 chain structure ~~of [[Factor inhibiting HIF]], [[Hypoxia-inducible factor prolyl hydroxylase]] and [[Prolyl hydroxylase domain]]~~ 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=3HQR OCA].	+	[[3hqr]] is a 2 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=3HQR OCA].

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

OCA at 06:51, 27 July 2012

OCA — Fri, 27 Jul 2012 06:51:22 GMT

←Older revision		Revision as of 06:51, 27 July 2012
Line 1:		Line 1:
	[[Image:3hqr.png\|left\|200px]]		[[Image:3hqr.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3hqr", 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_3hqr\| PDB=3hqr \| SCENE= }}		{{STRUCTURE_3hqr\| PDB=3hqr \| SCENE= }}

	===PHD2:Mn:NOG:HIF1-alpha substrate complex===		===PHD2:Mn:NOG:HIF1-alpha substrate complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19604478}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19604478 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19604478}}		{{ABSTRACT_PUBMED_19604478}}

	==About this Structure==		==About this Structure==
-	[[3hqr]] is a 2 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=3HQR OCA].	+	[[3hqr]] is a 2 chain structure of [[Factor inhibiting HIF]], [[Hypoxia-inducible factor prolyl hydroxylase]] and [[Prolyl hydroxylase domain]] 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=3HQR OCA].
		+
		+	==See Also==
		+	*[[Factor inhibiting HIF\|Factor inhibiting HIF]]
		+	*[[Hypoxia-inducible factor prolyl hydroxylase\|Hypoxia-inducible factor prolyl hydroxylase]]
		+	*[[Prolyl hydroxylase domain\|Prolyl hydroxylase domain]]

	==Reference==		==Reference==
Line 28:		Line 22:
	[[Category: Schofield, C J.]]		[[Category: Schofield, C J.]]
	[[Category: Activator]]		[[Category: Activator]]
-	[[Category: Alternative splicing]]
	[[Category: Congenital erythrocytosis]]		[[Category: Congenital erythrocytosis]]
-	[[Category: Cytoplasm]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
Line 41:		Line 33:
	[[Category: Nucleus]]		[[Category: Nucleus]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-	[[Category: Oxidoreductase/transcription complex]]	+	[[Category: Oxidoreductase-transcription complex]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
	[[Category: S-nitrosylation]]		[[Category: S-nitrosylation]]
	[[Category: Transcription]]		[[Category: Transcription]]
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
-	[[Category: Ubl conjugation]]
	[[Category: Vitamin c]]		[[Category: Vitamin c]]
-	[[Category: Zinc]]
	[[Category: Zinc-finger]]		[[Category: Zinc-finger]]

OCA at 11:45, 26 May 2011

OCA — Thu, 26 May 2011 11:45:13 GMT

←Older revision		Revision as of 11:45, 26 May 2011
Line 22:		Line 22:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19604478~~</ref><ref group="xtra">PMID:~~16782814~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019604478</ref><ref group="xtra">PMID:016782814</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chowdhury, R.]]		[[Category: Chowdhury, R.]]

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

OCA — Mon, 14 Mar 2011 18:02:00 GMT

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

←Older revision

Revision as of 18:02, 14 March 2011

OCA at 18:01, 14 March 2011

OCA — Mon, 14 Mar 2011 18:01:57 GMT

←Older revision		Revision as of 18:01, 14 March 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3hqr.png\|left\|200px]]

-	The ~~entry 3hqr~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3hqr", 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_3hqr\| PDB=3hqr \| SCENE= }}

-	~~Authors~~: ~~Chowdhury, R., McDonough, M.A., Schofield, C.J.~~	+	===PHD2:Mn:NOG:HIF1-alpha substrate complex===

-	Description: PHD2:Mn:NOG:HIF1-alpha substrate complex

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Jun 17 09~~:48:~~13 2009''~~	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19604478}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19604478 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19604478}}
		+
		+	==About this Structure==
		+	[[3hqr]] is a 2 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=3HQR OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19604478</ref><ref group="xtra">PMID:16782814</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Chowdhury, R.]]
		+	[[Category: McDonough, M A.]]
		+	[[Category: Schofield, C J.]]
		+	[[Category: Activator]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Congenital erythrocytosis]]
		+	[[Category: Cytoplasm]]
		+	[[Category: Dioxygenase]]
		+	[[Category: Disease mutation]]
		+	[[Category: Dna-binding]]
		+	[[Category: Double stranded beta-helix]]
		+	[[Category: Hydroxylation]]
		+	[[Category: Iron]]
		+	[[Category: Isopeptide bond]]
		+	[[Category: Metal-binding]]
		+	[[Category: Nucleus]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase/transcription complex]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
		+	[[Category: S-nitrosylation]]
		+	[[Category: Transcription]]
		+	[[Category: Transcription regulation]]
		+	[[Category: Ubl conjugation]]
		+	[[Category: Vitamin c]]
		+	[[Category: Zinc]]
		+	[[Category: Zinc-finger]]