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4wn5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the C-terminal Per-Arnt-Sim (PASb) of human HIF-3alpha9 bound to 18:1-1-monoacylglycerol== | |
| + | <StructureSection load='4wn5' size='340' side='right'caption='[[4wn5]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wn5]] 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=4WN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WN5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MVC:MONOVACCENIN'>MVC</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4wn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wn5 OCA], [https://pdbe.org/4wn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wn5 RCSB], [https://www.ebi.ac.uk/pdbsum/4wn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wn5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HIF3A_HUMAN HIF3A_HUMAN] Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422). Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity).[UniProtKB:Q0VBL6]<ref>PMID:11573933</ref> <ref>PMID:16126907</ref> <ref>PMID:19694616</ref> <ref>PMID:20416395</ref> <ref>PMID:21069422</ref> Isoform 2: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Also inhibits hypoxia-inducible ARNT-mediated gene expression.<ref>PMID:11573933</ref> Isoform 3: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.<ref>PMID:19694616</ref> <ref>PMID:20416395</ref> <ref>PMID:21069422</ref> isoform 4: Attenuates the ability of transcription factor HIF1A and EPAS1/HIF2A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation (PubMed:16126907, PubMed:17998805, PubMed:19694616, PubMed:20416395). May act as a tumor suppressor and inhibits malignant cell transformation (PubMed:17998805).<ref>PMID:16126907</ref> <ref>PMID:17998805</ref> <ref>PMID:19694616</ref> <ref>PMID:20416395</ref> Isoform 5: Attenuates the ability of transcription factor HIF1A to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation.<ref>PMID:21069422</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hypoxia-inducible transcription factors (HIF) form heterodimeric complexes that mediate cell responses to hypoxia. The oxygen-dependent stability and activity of the HIF-alpha subunits is traditionally associated to post-translational modifications such as hydroxylation, acetylation, ubiquitination, and phosphorylation. Here we report novel evidence showing that unsaturated fatty acids are naturally occurring, non-covalent structural ligands of HIF-3alpha, thus providing the initial framework for exploring its exceptional role as a lipid sensor under hypoxia. | ||
| - | + | Unsaturated fatty acids as high-affinity ligands of the C-terminal Per-ARNT-Sim domain from the Hypoxia-inducible factor 3alpha.,Fala AM, Oliveira JF, Adamoski D, Aricetti JA, Dias MM, Dias MVB, Sforca ML, Lopes-de-Oliveira PS, Rocco SA, Caldana C, Dias SMG, Ambrosio ALB Sci Rep. 2015 Aug 3;5:12698. doi: 10.1038/srep12698. PMID:26237540<ref>PMID:26237540</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4wn5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ambrosio AL]] | ||
| + | [[Category: Dias SM]] | ||
| + | [[Category: Fala AM]] | ||
| + | [[Category: Oliveira JF]] | ||
Current revision
Crystal structure of the C-terminal Per-Arnt-Sim (PASb) of human HIF-3alpha9 bound to 18:1-1-monoacylglycerol
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