4nr1 - Revision history

OCA at 17:01, 20 September 2023

OCA — Wed, 20 Sep 2023 17:01:54 GMT

←Older revision		Revision as of 17:01, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nr1]] 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nr1]] 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.68Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [https://pdbe.org/4nr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [https://pdbe.org/4nr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:43, 11 January 2023

OCA — Wed, 11 Jan 2023 08:43:40 GMT

←Older revision		Revision as of 08:43, 11 January 2023
Line 3:		Line 3:
	<StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>		<StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nr1]] 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nr1]] 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~OGA~~:N-~~OXALYLGLYCINE~~'>~~OGA~~</scene>, <scene name='pdbligand=~~SO4~~:~~SULFATE+ION~~'>~~SO4~~</scene>, <scene name='pdbligand=ZN:~~ZINC~~+ION'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=~~DYL~~:~~(2R)-2-AMINOPENT-4-ENOIC~~+~~ACID~~'>~~DYL~~</scene~~></td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [https://pdbe.org/4nr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FIH1, HIF1AN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [~~http~~://pdbe.org/4nr1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>	+	[https://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>

	==See Also==		==See Also==
Line 20:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Hypoxia-inducible factor-asparagine dioxygenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: McDonough~~, M A~~]]	+	[[Category: McDonough MA]]
-	[[Category: Schofield~~, C J~~]]	+	[[Category: Schofield CJ]]
-	[[Category: Scotti~~, J S]]~~	+	[[Category: Scotti JS]]
-	~~[[Category: Activator-inhibitor]]~~	+
-	~~[[Category: Ard]]~~	+
-	~~[[Category: Asparaginyl/aspartyl hydroxylase]]~~	+
-	~~[[Category: Beta-hydroxylation]]~~	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Dsbh]]~~	+
-	~~[[Category: Epigenetic regulation]]~~	+
-	~~[[Category: Facial triad]]~~	+
-	~~[[Category: Helix-loop-helix-beta]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: On-heme]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase-peptide complex]]~~	+
-	~~[[Category: Oxygenase]]~~	+
-	~~[[Category: Signaling]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 08:45, 10 April 2019

OCA — Wed, 10 Apr 2019 08:45:38 GMT

←Older revision		Revision as of 08:45, 10 April 2019
Line 1:		Line 1:

	==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==		==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
-	<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>	+	<StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nr1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nr1]] 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FIH1, HIF1AN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
Line 19:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Hypoxia-inducible factor-asparagine dioxygenase]]		[[Category: Hypoxia-inducible factor-asparagine dioxygenase]]
		+	[[Category: Large Structures]]
	[[Category: McDonough, M A]]		[[Category: McDonough, M A]]
	[[Category: Schofield, C J]]		[[Category: Schofield, C J]]

OCA at 16:54, 2 January 2017

OCA — Mon, 02 Jan 2017 16:54:33 GMT

←Older revision		Revision as of 16:54, 2 January 2017
Line 1:		Line 1:
		+
	==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==		==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
	<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>		<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>		[[http://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>
		+
		+	==See Also==
		+	*[[Factor inhibiting HIF\|Factor inhibiting HIF]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:02, 12 February 2015

OCA — Thu, 12 Feb 2015 06:02:17 GMT

←Older revision		Revision as of 06:02, 12 February 2015
Line 1:		Line 1:
-	==~~Structure of an oxygenase~~ in complex with ~~substrate~~==	+	==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide==
	<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>		<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 19:		Line 19:
	[[Category: Schofield, C J]]		[[Category: Schofield, C J]]
	[[Category: Scotti, J S]]		[[Category: Scotti, J S]]
-	[[Category: 2-oxoglutarate]]
	[[Category: Activator-inhibitor]]		[[Category: Activator-inhibitor]]
	[[Category: Ard]]		[[Category: Ard]]
-	[[Category: Asparaginyl/ aspartyl hydroxylase]]	+	[[Category: Asparaginyl/aspartyl hydroxylase]]
	[[Category: Beta-hydroxylation]]		[[Category: Beta-hydroxylation]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
Line 30:		Line 29:
	[[Category: Facial triad]]		[[Category: Facial triad]]
	[[Category: Helix-loop-helix-beta]]		[[Category: Helix-loop-helix-beta]]
-	[[Category: Iron]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
	[[Category: On-heme]]		[[Category: On-heme]]

OCA at 16:56, 21 January 2015

OCA — Wed, 21 Jan 2015 16:56:50 GMT

←Older revision		Revision as of 16:56, 21 January 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of an oxygenase in complex with substrate==
-		+	<StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution\|resolution]] 2.68Å' scene=''>
-	~~The entry~~ 4nr1 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4nr1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br>
-	~~Authors~~: ~~Scotti~~, J.S., ~~McDonough~~, M.A., ~~Schofield, C~~.J.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr>
-	~~Description~~: ~~Structure of~~ an ~~oxygenase~~ in ~~complex~~ with ~~substrate~~	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4jaa\|4jaa]]</td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </span></td></tr>
-	[[Category: ~~Mcdonough~~, M.A]]	+	<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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum]</span></td></tr>
-	[[Category: ~~Scotti~~, J.S]]	+	</table>
-	[[Category: ~~Schofield~~, C.J]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hypoxia-inducible factor-asparagine dioxygenase]]
		+	[[Category: McDonough, M A]]
		+	[[Category: Schofield, C J]]
		+	[[Category: Scotti, J S]]
		+	[[Category: 2-oxoglutarate]]
		+	[[Category: Activator-inhibitor]]
		+	[[Category: Ard]]
		+	[[Category: Asparaginyl/ aspartyl hydroxylase]]
		+	[[Category: Beta-hydroxylation]]
		+	[[Category: Dioxygenase]]
		+	[[Category: Dna-binding]]
		+	[[Category: Dsbh]]
		+	[[Category: Epigenetic regulation]]
		+	[[Category: Facial triad]]
		+	[[Category: Helix-loop-helix-beta]]
		+	[[Category: Iron]]
		+	[[Category: Metal-binding]]
		+	[[Category: On-heme]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase-peptide complex]]
		+	[[Category: Oxygenase]]
		+	[[Category: Signaling]]
		+	[[Category: Transcription]]

OCA at 14:14, 24 December 2014

OCA — Wed, 24 Dec 2014 14:14:08 GMT

←Older revision		Revision as of 14:14, 24 December 2014
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	Description: Structure of an oxygenase in complex with substrate		Description: Structure of an oxygenase in complex with substrate
		+	[[Category: Unreleased Structures]]
		+	[[Category: Mcdonough, M.A]]
		+	[[Category: Scotti, J.S]]
		+	[[Category: Schofield, C.J]]

OCA at 10:19, 5 February 2014

OCA — Wed, 05 Feb 2014 10:19:32 GMT

←Older revision		Revision as of 10:19, 5 February 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4nr1 is ON HOLD	+	The entry 4nr1 is ON HOLD until Paper Publication

	Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J.		Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J.

	Description: Structure of an oxygenase in complex with substrate		Description: Structure of an oxygenase in complex with substrate

OCA: Protected "4nr1" [edit=sysop:move=sysop]

OCA — Wed, 04 Dec 2013 06:53:09 GMT

Protected "4nr1" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:53, 4 December 2013

OCA: New page: '''Unreleased structure''' The entry 4nr1 is ON HOLD Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J. Description: Structure of an oxygenase in complex with substrate

OCA — Wed, 04 Dec 2013 06:53:08 GMT

New page: '''Unreleased structure''' The entry 4nr1 is ON HOLD Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J. Description: Structure of an oxygenase in complex with substrate

New page

'''Unreleased structure'''

The entry 4nr1 is ON HOLD

Authors: Scotti, J.S., McDonough, M.A., Schofield, C.J.

Description: Structure of an oxygenase in complex with substrate