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5op8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Factor Inhibiting HIF (FIH) in complex with zinc and Molidustat== | |
| - | + | <StructureSection load='5op8' size='340' side='right' caption='[[5op8]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5op8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OP8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A1H:2-(6-morpholin-4-ylpyrimidin-4-yl)-4-(1,2,3-triazol-1-yl)-1~{H}-pyrazol-3-one'>A1H</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <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=5op8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5op8 OCA], [http://pdbe.org/5op8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5op8 RCSB], [http://www.ebi.ac.uk/pdbsum/5op8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5op8 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == 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: Clifton, I J]] | ||
| + | [[Category: Leissing, T M]] | ||
| + | [[Category: Lu, X]] | ||
| + | [[Category: Schofield, C J]] | ||
| + | [[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]] | ||
Revision as of 07:12, 18 October 2017
Factor Inhibiting HIF (FIH) in complex with zinc and Molidustat
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Categories: Clifton, I J | Leissing, T M | Lu, X | Schofield, C J | Activator-inhibitor | Ard | Asparaginyl/aspartyl hydroxylase | Beta-hydroxylation | Dioxygenase | Dna-binding | Dsbh | Epigenetic regulation | Facial triad | Helix-loop-helix-beta | Metal-binding | On-heme | Oxidoreductase | Oxidoreductase-peptide complex | Oxygenase | Signaling | Transcription
