View source for 3ohv


==Crystal structure of the human Bach2 POZ domain, form II==
<StructureSection load='3ohv' size='340' side='right'caption='[[3ohv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ohv]] is a 6 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=3OHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OHV 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]] 2.2&#8491;</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=3ohv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ohv OCA], [https://pdbe.org/3ohv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ohv RCSB], [https://www.ebi.ac.uk/pdbsum/3ohv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ohv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BACH2_HUMAN BACH2_HUMAN] Transcriptional regulator that acts as repressor or activator. Binds to Maf recognition elements (MARE). Play important roles in coordinating transcription activation and repression by MAFK (By similarity). Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1.<ref>PMID:17018862</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bach2 is a transcriptional repressor that is expressed during specific stages of B-cell development and in neuronal cells. It plays a critical role in modulating class-switch recombination during the differentiation of mature B cells to antibody-secreting plasma cells and it is also an important regulator of apoptotic responses to oxidative stress. Bach2 has been implicated both as an oncogene and as a tumour suppressor in human malignancy. The interaction of Bach2 with its target genes is mediated via its basic leucine-zipper region, whereas the N-terminal POZ domain recruits transcriptional co-repressors and class II histone deacetylases. Here, the crystal structure of the human Bach2 POZ domain is reported at 2.1 A resolution. The Bach2 POZ-domain dimer resembles the POZ-domain dimers of the POZ zinc finger transcription factors and dimerization is independent of an N-terminal region that has previously been implicated in the dimerization of the POZ basic leucine-zipper protein Bach1. The Bach2 POZ domain crystallized in two forms which differed by the presence of an intersubunit disulfide bond. The intersubunit disulfide bond is present both in bacterially expressed Bach2 POZ domain in solution and in protein expressed in transfected eukaryotic cells. These crystal structures will be relevant for understanding the regulation of Bach2 in response to oxidative stress and for the design of therapeutics that target the Bach2 POZ domain in human malignancy.

The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond.,Rosbrook GO, Stead MA, Carr SB, Wright SC Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):26-34. Epub 2011 Dec 9. PMID:22194330<ref>PMID:22194330</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ohv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carr SB]]
[[Category: Rosbrook GO]]
[[Category: Stead MA]]
[[Category: Wright SC]]