5v0l: Difference between revisions

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 ==Crystal structure of the AHR-ARNT heterodimer in complex with the DRE==
-<StructureSection load='5v0l' size='340' side='right' caption='[[5v0l]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
+<StructureSection load='5v0l' size='340' side='right'caption='[[5v0l]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5v0l]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V0L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5v0l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V0L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 4&#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=5v0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v0l OCA], [http://pdbe.org/5v0l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v0l RCSB], [http://www.ebi.ac.uk/pdbsum/5v0l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v0l ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5v0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v0l OCA], [https://pdbe.org/5v0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v0l RCSB], [https://www.ebi.ac.uk/pdbsum/5v0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v0l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ARNT_HUMAN ARNT_HUMAN]] Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia. [[http://www.uniprot.org/uniprot/AHR_MOUSE AHR_MOUSE]] Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues.<ref>PMID:1314586</ref> <ref>PMID:7961644</ref> <ref>PMID:7969080</ref> <ref>PMID:8806883</ref> <ref>PMID:9427285</ref> <ref>PMID:10973493</ref> <ref>PMID:10639156</ref>
+[https://www.uniprot.org/uniprot/ARNT_HUMAN ARNT_HUMAN] Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5v0l" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bradfield, C A]]
+[[Category: Homo sapiens]]
-[[Category: Jiang, L]]
+[[Category: Large Structures]]
-[[Category: Lee, W]]
+[[Category: Mus musculus]]
-[[Category: Seok, S H]]
+[[Category: Bradfield CA]]
-[[Category: Xing, Y]]
+[[Category: Jiang L]]
-[[Category: Ahr]]
+[[Category: Lee W]]
-[[Category: Arnt]]
+[[Category: Seok S-H]]
-[[Category: Heterodimer]]
+[[Category: Xing Y]]
-[[Category: Transcription factor]]
-[[Category: Transcription-dna complex]]