4z2w

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'''Unreleased structure'''
 
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The entry 4z2w is ON HOLD until Paper Publication
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==Factor Inhibiting HIF in Complex with Fe, and Alpha-Ketoglutarate==
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<StructureSection load='4z2w' size='340' side='right'caption='[[4z2w]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4z2w]] 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=4Z2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z2W FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4z2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z2w OCA], [https://pdbe.org/4z2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z2w RCSB], [https://www.ebi.ac.uk/pdbsum/4z2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z2w ProSAT]</span></td></tr>
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</table>
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== Function ==
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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>
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Authors: Taabazuing, C.Y., Garman, S.C., Knapp, M.J.
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==See Also==
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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Description: Factor Inhibiting HIF in Complex with Fe, and Alpha-Ketoglutarate
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*[[Hypoxia-Inducible factor 1 alpha inhibitor|Hypoxia-Inducible factor 1 alpha inhibitor]]
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[[Category: Unreleased Structures]]
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== References ==
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[[Category: Taabazuing, C.Y]]
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<references/>
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[[Category: Knapp, M.J]]
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__TOC__
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[[Category: Garman, S.C]]
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Garman SC]]
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[[Category: Knapp MJ]]
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[[Category: Taabazuing CY]]

Current revision

Factor Inhibiting HIF in Complex with Fe, and Alpha-Ketoglutarate

PDB ID 4z2w

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