5vpc: Difference between revisions
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==Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal== | |||
<StructureSection load='5vpc' size='340' side='right'caption='[[5vpc]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.498Å</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=NA:SODIUM+ION'>NA</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=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> | |||
== 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5vpc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Metallothiol transferase FosB|Metallothiol transferase FosB]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Machius MC]] | |||
[[Category: Rudenko G]] | |||
[[Category: Yin Z]] | |||
Latest revision as of 13:54, 4 October 2023
Transcription factor FosB/JunD bZIP domain in its oxidized form, type-II crystal
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