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==Crystal Structure of BAZ2B bromodomain in complex with 1-methylpyridinone compound 4== | |||
<StructureSection load='6fgu' size='340' side='right' caption='[[6fgu]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fgu]] is a 1 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=6FGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FGU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D9Q:1-methyl-6-oxidanylidene-~{N}-(2-pyrrolidin-1-ylethyl)pyridine-3-carboxamide'>D9Q</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fg6|6fg6]], [[6fgf|6fgf]], [[6fgg|6fgg]], [[6fgh|6fgh]], [[6fgi|6fgi]], [[6fgt|6fgt]]</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=6fgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fgu OCA], [http://pdbe.org/6fgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fgu RCSB], [http://www.ebi.ac.uk/pdbsum/6fgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fgu 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 == | |||
The bromodomain-containing protein BAZ2A is a validated target in prostate cancer, while the function of its paralog BAZ2B is still undefined. The bromodomains of BAZ2A and BAZ2B have a very similar binding site for their natural ligand, the acetylated lysine side chain. Here, we present an analysis of the binding modes of eight compounds belonging to three distinct chemical classes. For all compounds, the moiety mimicking the natural ligand makes essentially identical interactions in the BAZ2A and BAZ2B bromodomains. In contrast, the rest of the molecule is partially solvent exposed and shows different orientations and interactions in the two bromodomains. Some of these differences could be exploited for designing selective inhibitors within the BAZ2 bromodomain subfamily. | |||
Structural Analysis of Small Molecule Binding to the BAZ2A and BAZ2B Bromodomains.,Dalle Vedove A, Spiliotopoulos D, D'Agostino VG, Marchand JR, Unzue A, Nevado C, Lolli G, Caflisch A ChemMedChem. 2018 May 17. doi: 10.1002/cmdc.201800234. PMID:29770599<ref>PMID:29770599</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6fgu" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Caflisch, A]] | |||
[[Category: Lolli, G]] | [[Category: Lolli, G]] | ||
[[Category: Spiliotopoulos, D]] | [[Category: Spiliotopoulos, D]] | ||
[[Category: | [[Category: Vedove, A Dalle]] | ||
[[Category: Four helical bundle]] | |||
[[Category: Transcription]] | |||
Latest revision as of 11:00, 29 August 2018
Crystal Structure of BAZ2B bromodomain in complex with 1-methylpyridinone compound 4Crystal Structure of BAZ2B bromodomain in complex with 1-methylpyridinone compound 4
Structural highlights
Function[BAZ2B_HUMAN] May play a role in transcriptional regulation interacting with ISWI. Publication Abstract from PubMedThe bromodomain-containing protein BAZ2A is a validated target in prostate cancer, while the function of its paralog BAZ2B is still undefined. The bromodomains of BAZ2A and BAZ2B have a very similar binding site for their natural ligand, the acetylated lysine side chain. Here, we present an analysis of the binding modes of eight compounds belonging to three distinct chemical classes. For all compounds, the moiety mimicking the natural ligand makes essentially identical interactions in the BAZ2A and BAZ2B bromodomains. In contrast, the rest of the molecule is partially solvent exposed and shows different orientations and interactions in the two bromodomains. Some of these differences could be exploited for designing selective inhibitors within the BAZ2 bromodomain subfamily. Structural Analysis of Small Molecule Binding to the BAZ2A and BAZ2B Bromodomains.,Dalle Vedove A, Spiliotopoulos D, D'Agostino VG, Marchand JR, Unzue A, Nevado C, Lolli G, Caflisch A ChemMedChem. 2018 May 17. doi: 10.1002/cmdc.201800234. PMID:29770599[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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