5tbm

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Current revision (12:57, 4 October 2023) (edit) (undo)
 
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<StructureSection load='5tbm' size='340' side='right'caption='[[5tbm]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='5tbm' size='340' side='right'caption='[[5tbm]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tbm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TBM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TBM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tbm]] 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=5TBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TBM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=79A:3-{[(1S)-2,2-DIFLUORO-1-HYDROXY-7-(METHYLSULFONYL)-2,3-DIHYDRO-1H-INDEN-4-YL]OXY}-5-FLUOROBENZONITRILE'>79A</scene></td></tr>
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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]] 1.85&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPAS1, BHLHE73, HIF2A, MOP2, PASD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ARNT, BHLHE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=79A:3-{[(1S)-2,2-DIFLUORO-1-HYDROXY-7-(METHYLSULFONYL)-2,3-DIHYDRO-1H-INDEN-4-YL]OXY}-5-FLUOROBENZONITRILE'>79A</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tbm OCA], [http://pdbe.org/5tbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tbm RCSB], [http://www.ebi.ac.uk/pdbsum/5tbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tbm ProSAT]</span></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=5tbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tbm OCA], [https://pdbe.org/5tbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tbm RCSB], [https://www.ebi.ac.uk/pdbsum/5tbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tbm ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/EPAS1_HUMAN EPAS1_HUMAN]] Defects in EPAS1 are the cause of familial erythrocytosis type 4 (ECYT4) [MIM:[http://omim.org/entry/611783 611783]]. ECYT4 is an autosomal dominant disorder characterized by increased serum red blood cell mass, elevated hemoglobin concentration and hematocrit, and normal platelet and leukocyte counts.<ref>PMID:19208626</ref> <ref>PMID:18378852</ref> <ref>PMID:18184961</ref> <ref>PMID:22367913</ref>
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/EPAS1_HUMAN EPAS1_HUMAN]] Transcription factor involved in the induction of oxygen regulated genes. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation seems to require recruitment of transcriptional coactivators such as CREBPB and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD. [[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.
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[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.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 5tbm" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5tbm" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Du, X]]
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[[Category: Du X]]
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[[Category: Hif2 inhibitor hif2 ligand pas-b hypoxia inducible factor 2 epas1]]
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[[Category: Transcription]]
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Current revision

Crystal structure of PT2385 bound to HIF2a-B*:ARNT-B* complex

PDB ID 5tbm

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