5e9i: Difference between revisions

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-'''Unreleased structure'''
-The entry 5e9i is ON HOLD
+==Crystal Structure of BAZ2B bromodomain in complex with fragment F60==
+<StructureSection load='5e9i' size='340' side='right'caption='[[5e9i]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5e9i]] is a 1 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=5E9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E9I 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]] 1.96&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F60:1H-INDOL-6-OL'>F60</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=5e9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9i OCA], [https://pdbe.org/5e9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e9i RCSB], [https://www.ebi.ac.uk/pdbsum/5e9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9i ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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 ==
+Bromodomains are protein modules that bind to acetylated lysine side chains in histones and other proteins. The bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) has been reported to be poorly druggable. Here, we screened an in-house library of 350 fragments by automatic docking to the BAZ2B bromodomain. The top 12 fragments according to the predicted binding energy were selected for experiments of soaking into apo crystals of BAZ2B which yielded the structure of the complex for four of them, which is a hit rate of 33%. Additional crystal structures were solved for BAZ2B and two scaffolds identified by analogy. For three topologically similar fragments, the crystal structures reveal binding modes with different penetration, i.e., with zero, one, and two water molecules, respectively, located between the fragment and the side chain of a conserved tyrosine (Tyr1901) in the bottom of the acetyl lysine pocket of BAZ2B. Furthermore, a remarkable stereoselectivity of the acetyl lysine pocket emerges from the crystal structures of the bromodomains of BAZ2B and SMARCA4 in complex with the chiral diol MPD (2-methyl-2,4-pentanediol).
-Authors: Lolli, G., Caflisch, A.
+High-Throughput Fragment Docking into the BAZ2B Bromodomain: Efficient in Silico Screening for X-Ray Crystallography.,Lolli G, Caflisch A ACS Chem Biol. 2016 Mar 18;11(3):800-7. doi: 10.1021/acschembio.5b00914. PMID:26942307<ref>PMID:26942307</ref>
-Description: Crystal Structure of BAZ2B bromodomain in complex with fragment F60
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lolli, G]]
+<div class="pdbe-citations 5e9i" style="background-color:#fffaf0;"></div>
-[[Category: Caflisch, A]]
+==See Also==
+*[[Bromodomain adjacent to zinc finger 3D structures|Bromodomain adjacent to zinc finger 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Caflisch A]]
+[[Category: Lolli G]]