2wa3

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==FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3-hydroxyphenyl)-2-oxoacetic acid==
==FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3-hydroxyphenyl)-2-oxoacetic acid==
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<StructureSection load='2wa3' size='340' side='right' caption='[[2wa3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='2wa3' size='340' side='right'caption='[[2wa3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2wa3]] 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=2WA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WA3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2wa3]] 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=2WA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WA3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A29:2-(3-HYDROXYPHENYL)-2-OXO-ETHANOIC+ACID'>A29</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wa4|2wa4]], [[1mze|1mze]], [[2w0x|2w0x]], [[2cgn|2cgn]], [[1mzf|1mzf]], [[1h2n|1h2n]], [[1yci|1yci]], [[2cgo|2cgo]], [[1h2k|1h2k]], [[1iz3|1iz3]], [[1h2l|1h2l]], [[1h2m|1h2m]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A29:2-(3-HYDROXYPHENYL)-2-OXO-ETHANOIC+ACID'>A29</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa3 OCA], [https://pdbe.org/2wa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wa3 RCSB], [https://www.ebi.ac.uk/pdbsum/2wa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wa3 ProSAT]</span></td></tr>
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<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=2wa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa3 OCA], [http://pdbe.org/2wa3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wa3 RCSB], [http://www.ebi.ac.uk/pdbsum/2wa3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wa3 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 2wa3" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2wa3" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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*[[Hypoxia-Inducible factor 1 alpha inhibitor|Hypoxia-Inducible factor 1 alpha inhibitor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Peptide-aspartate beta-dioxygenase]]
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[[Category: Large Structures]]
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[[Category: Clifton, I J]]
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[[Category: Clifton IJ]]
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[[Category: Conejo-Garcia, A]]
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[[Category: Conejo-Garcia A]]
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[[Category: Lienard, B M.R]]
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[[Category: Lienard BMR]]
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[[Category: McDonough, M A]]
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[[Category: McDonough MA]]
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[[Category: Schofield, C J]]
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[[Category: Schofield CJ]]
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[[Category: Dioxygenase]]
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[[Category: Hydroxylase]]
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[[Category: Hypoxia]]
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[[Category: Oxidoreductase]]
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[[Category: Transcription]]
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[[Category: Transcription activator/inhibitor]]
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Current revision

FACTOR INHIBITING HIF-1 ALPHA WITH 2-(3-hydroxyphenyl)-2-oxoacetic acid

PDB ID 2wa3

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