6uci: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6uci is ON HOLD  until Paper Publication
+==Transcription factor DeltaFosB bZIP domain self-assembly, oxidized form==
+<StructureSection load='6uci' size='340' side='right'caption='[[6uci]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6uci]] 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=6UCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UCI 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]] 2.09&#8491;</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></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=6uci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uci OCA], [https://pdbe.org/6uci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uci RCSB], [https://www.ebi.ac.uk/pdbsum/6uci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uci 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 ==
+DeltaFosB is a highly stable transcription factor that accumulates in specific brain regions upon chronic exposure to drugs of abuse, stress, or seizures, and mediates lasting behavioral responses. DeltaFosB reportedly heterodimerizes with JunD forming a canonical bZIP leucine zipper coiled coil that clamps onto DNA. However, the striking accumulation of DeltaFosB protein in brain upon chronic insult has brought its molecular status into question. Here, we demonstrate through a series of crystal structures that the DeltaFosB bZIP domain self-assembles into stable oligomeric assemblies that defy the canonical arrangement. The DeltaFosB bZIP domain also self-assembles in solution, and in neuron-like Neuro 2a cells it is trapped into molecular arrangements that are consistent with our structures. Our data suggest that, as DeltaFosB accumulates in brain in response to chronic insult, it forms non-canonical assemblies. These species may be at the root of DeltaFosB's striking protein stability, and its unique transcriptional and behavioral consequences.
-Authors:
+Self-assembly of the bZIP transcription factor DeltaFosB.,Yin Z, Venkannagari H, Lynch H, Aglyamova G, Bhandari M, Machius M, Nestler EJ, Robison AJ, Rudenko G Curr Res Struct Biol. 2020;2:1-13. doi: 10.1016/j.crstbi.2019.12.001. Epub 2019, Dec 24. PMID:32542236<ref>PMID:32542236</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6uci" 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 M]]
+[[Category: Rudenko G]]
+[[Category: Yin Z]]