5op6

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m (Protected "5op6" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5op6 is ON HOLD until Paper Publication
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==Factor Inhibiting HIF (FIH) in complex with zinc and GSK128863==
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<StructureSection load='5op6' size='340' side='right' caption='[[5op6]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5op6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OP6 FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A0W:2-[[1,3-dicyclohexyl-4-oxidanyl-2,6-bis(oxidanylidene)pyrimidin-5-yl]carbonylamino]ethanoic+acid'>A0W</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>
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[[Category: Unreleased Structures]]
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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=5op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5op6 OCA], [http://pdbe.org/5op6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5op6 RCSB], [http://www.ebi.ac.uk/pdbsum/5op6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5op6 ProSAT]</span></td></tr>
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</table>
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== 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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Clifton, I J]]
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[[Category: Leissing, T M]]
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[[Category: Lu, X]]
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[[Category: Schofield, C J]]
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[[Category: Thinnes, C C]]
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[[Category: Activator-inhibitor]]
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[[Category: Ard]]
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[[Category: Asparaginyl/aspartyl hydroxylase]]
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[[Category: Beta-hydroxylation]]
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[[Category: Dioxygenase]]
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[[Category: Dna-binding]]
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[[Category: Dsbh]]
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[[Category: Epigenetic regulation]]
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[[Category: Facial triad]]
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[[Category: Helix-loop-helix-beta]]
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[[Category: Metal-binding]]
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[[Category: On-heme]]
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[[Category: Oxidoreductase]]
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[[Category: Oxidoreductase-peptide complex]]
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[[Category: Oxygenase]]
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[[Category: Signaling]]
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[[Category: Transcription]]

Revision as of 07:12, 18 October 2017

Factor Inhibiting HIF (FIH) in complex with zinc and GSK128863

5op6, resolution 2.45Å

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