6ruj

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(New page: '''Unreleased structure''' The entry 6ruj is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures)
Current revision (12:28, 24 January 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6ruj is ON HOLD until Paper Publication
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==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)3-hydroxy-Leu peptide==
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<StructureSection load='6ruj' size='340' side='right'caption='[[6ruj]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ruj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RUJ 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]] 2.42&#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=KJW:(d)3-hydroxy-Leucine'>KJW</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>
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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=6ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ruj OCA], [https://pdbe.org/6ruj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ruj RCSB], [https://www.ebi.ac.uk/pdbsum/6ruj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ruj 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:
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==See Also==
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*[[Factor inhibiting HIF|Factor inhibiting HIF]]
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Description:
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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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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: McDonough MA]]
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[[Category: Nakashima Y]]
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[[Category: Schofield CJ]]

Current revision

Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)3-hydroxy-Leu peptide

PDB ID 6ruj

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