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5vpc

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==Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal==
==Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal==
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<StructureSection load='5vpc' size='340' side='right' caption='[[5vpc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='5vpc' size='340' side='right'caption='[[5vpc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vpc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VPC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vpc]] is a 4 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=5VPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VPC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.498&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vpa|5vpa]], [[5vpd|5vpd]], [[5vpe|5vpe]], [[5vpf|5vpf]], [[5vpb|5vpb]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<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=5vpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vpc OCA], [http://pdbe.org/5vpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vpc RCSB], [http://www.ebi.ac.uk/pdbsum/5vpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vpc 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=5vpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vpc OCA], [https://pdbe.org/5vpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vpc RCSB], [https://www.ebi.ac.uk/pdbsum/5vpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vpc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FOSB_HUMAN FOSB_HUMAN]] FosB interacts with Jun proteins enhancing their DNA binding activity. [[http://www.uniprot.org/uniprot/JUND_HUMAN JUND_HUMAN]] Transcription factor binding AP-1 sites.<ref>PMID:9989505</ref>
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[https://www.uniprot.org/uniprot/FOSB_HUMAN FOSB_HUMAN] FosB interacts with Jun proteins enhancing their DNA binding activity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The transcription factor, activator protein-1 (AP-1), binds to cognate DNA under redox control; yet, the underlying mechanism has remained enigmatic. A series of crystal structures of the AP-1 FosB/JunD bZIP domains reveal ordered DNA-binding regions in both FosB and JunD even in absence DNA. However, while JunD is competent to bind DNA, the FosB bZIP domain must undergo a large conformational rearrangement that is controlled by a 'redox switch' centered on an inter-molecular disulfide bond. Solution studies confirm that FosB/JunD cannot undergo structural transition and bind DNA when the redox-switch is in the 'OFF' state, and show that the mid-point redox potential of the redox switch affords it sensitivity to cellular redox homeostasis. The molecular and structural studies presented here thus reveal the mechanism underlying redox-regulation of AP-1 Fos/Jun transcription factors and provide structural insight for therapeutic interventions targeting AP-1 proteins.
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Activator Protein-1: redox switch controlling structure and DNA-binding.,Yin Z, Machius M, Nestler EJ, Rudenko G Nucleic Acids Res. 2017 Sep 7. doi: 10.1093/nar/gkx795. PMID:28981703<ref>PMID:28981703</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5vpc" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Metallothiol transferase FosB|Metallothiol transferase FosB]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Machius, M C]]
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[[Category: Homo sapiens]]
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[[Category: Rudenko, G]]
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[[Category: Large Structures]]
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[[Category: Yin, Z]]
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[[Category: Machius MC]]
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[[Category: Activator protein-1]]
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[[Category: Rudenko G]]
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[[Category: Basic leucine zipper]]
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[[Category: Yin Z]]
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[[Category: Bzip]]
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[[Category: Coiled-coil]]
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[[Category: Dna-binding protein]]
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[[Category: Fo]]
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[[Category: Jun]]
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[[Category: Redox switch]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal

PDB ID 5vpc

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