6hl5: Difference between revisions

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<StructureSection load='6hl5' size='340' side='right'caption='[[6hl5]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
<StructureSection load='6hl5' size='340' side='right'caption='[[6hl5]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6hl5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HL5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6hl5]] is a 2 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=6HL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HL5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
<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=6hl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hl5 OCA], [http://pdbe.org/6hl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hl5 RCSB], [http://www.ebi.ac.uk/pdbsum/6hl5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hl5 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hl5 OCA], [https://pdbe.org/6hl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hl5 RCSB], [https://www.ebi.ac.uk/pdbsum/6hl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hl5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> [[http://www.uniprot.org/uniprot/ASPP1_HUMAN ASPP1_HUMAN]] Regulator that plays a central role in regulation of apoptosis via its interaction with p53/TP53. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo.<ref>PMID:11684014</ref> 
[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>  
 
==See Also==
*[[Factor inhibiting HIF|Factor inhibiting HIF]]
*[[Hypoxia-Inducible factor 1 alpha inhibitor|Hypoxia-Inducible factor 1 alpha inhibitor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chowdhury, R]]
[[Category: Chowdhury R]]
[[Category: Clifton, I J]]
[[Category: Clifton IJ]]
[[Category: Leissing, T M]]
[[Category: Leissing TM]]
[[Category: Lu, X]]
[[Category: Lu X]]
[[Category: Schofield, C J]]
[[Category: Schofield CJ]]
[[Category: Activator-inhibitor]]
[[Category: Ank repeat]]
[[Category: Ankyrin repeat domain]]
[[Category: Ankyrin repeat]]
[[Category: Apoptosis]]
[[Category: Ard]]
[[Category: Asparaginyl/aspartyl hydroxylase]]
[[Category: Beta-hydroxylation]]
[[Category: Dioxygenase]]
[[Category: Double stranded beta-helix]]
[[Category: Dsbh]]
[[Category: Epigenetic regulation]]
[[Category: Facial triad]]
[[Category: Gene regulation]]
[[Category: Metal-binding]]
[[Category: Non-heme]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-peptide complex]]
[[Category: Oxygenase]]
[[Category: P53 binding protein]]
[[Category: Sh3 domain]]
[[Category: Signaling]]
[[Category: Transcription]]

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