View source for 6fhq


==Crystal structure of human BAZ2B PHD zinc finger in complex with Fr 21==
<StructureSection load='6fhq' size='340' side='right' caption='[[6fhq]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fhq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FHQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DE5:2-azanyl-~{N}-(1,3-thiazol-2-yl)ethanamide'>DE5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAZ2B, KIAA1476 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<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=6fhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fhq OCA], [http://pdbe.org/6fhq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fhq RCSB], [http://www.ebi.ac.uk/pdbsum/6fhq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fhq ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/BAZ2B_HUMAN BAZ2B_HUMAN]] May play a role in transcriptional regulation interacting with ISWI. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant homeodomain (PHD) zinc fingers are histone reader domains that are often associated with human diseases. Despite this, they constitute a poorly targeted class of readers, suggesting low ligandability. Here, we describe a successful fragment-based campaign targeting PHD fingers from the proteins BAZ2A and BAZ2B as model systems. We validated a pool of in silico fragments both biophysically and structurally and solved the first crystal structures of PHD zinc fingers in complex with fragments bound to an anchoring pocket at the histone binding site. The best-validated hits were found to displace a histone H3 tail peptide in competition assays. This work identifies new chemical scaffolds that provide suitable starting points for future ligand optimization using structure-guided approaches. The demonstrated ligandability of the PHD reader domains could pave the way for the development of chemical probes to drug this family of epigenetic readers.

Targeting Ligandable Pockets on Plant Homeodomain (PHD) Zinc Finger Domains by a Fragment-Based Approach.,Amato A, Lucas X, Bortoluzzi A, Wright D, Ciulli A ACS Chem Biol. 2018 Mar 20. doi: 10.1021/acschembio.7b01093. PMID:29529862<ref>PMID:29529862</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fhq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Amato, A]]
[[Category: Bortoluzzi, A]]
[[Category: Ciulli, A]]
[[Category: Lucas, X]]
[[Category: Wright, D]]
[[Category: Baz2a]]
[[Category: Baz2b]]
[[Category: Bromodomain]]
[[Category: Competition]]
[[Category: Epigenetic]]
[[Category: Fragment]]
[[Category: Phd]]
[[Category: Transcription]]
[[Category: Zinc finger]]