5vpf
From Proteopedia
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==Transcription factor FosB/JunD bZIP domain in complex with cognate DNA, type-II crystal== | ==Transcription factor FosB/JunD bZIP domain in complex with cognate DNA, type-II crystal== | ||
| - | <StructureSection load='5vpf' size='340' side='right' caption='[[5vpf]], [[Resolution|resolution]] 2.69Å' scene=''> | + | <StructureSection load='5vpf' size='340' side='right'caption='[[5vpf]], [[Resolution|resolution]] 2.69Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5vpf]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VPF OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5vpf]] is a 8 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=5VPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VPF FirstGlance]. <br> |
| - | </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.694Å</td></tr> |
| - | + | <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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vpf OCA], [https://pdbe.org/5vpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vpf RCSB], [https://www.ebi.ac.uk/pdbsum/5vpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vpf ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FOSB_HUMAN FOSB_HUMAN] FosB interacts with Jun proteins enhancing their DNA binding activity. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5vpf" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Metallothiol transferase FosB|Metallothiol transferase FosB]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Machius M]] |
| - | [[Category: | + | [[Category: Rudenko G]] |
| - | [[Category: | + | [[Category: Yin Z]] |
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Current revision
Transcription factor FosB/JunD bZIP domain in complex with cognate DNA, type-II crystal
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