4nr9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nr9]] 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=4NR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nr9]] 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=4NR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NR9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=4nr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr9 OCA], [https://pdbe.org/4nr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr9 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr9 ProSAT]</span></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=4nr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr9 OCA], [https://pdbe.org/4nr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nr9 RCSB], [https://www.ebi.ac.uk/pdbsum/4nr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 20:02, 20 September 2023
Crystal Structure of the bromodomain of human BAZ2B in complex with acetylated lysineCrystal Structure of the bromodomain of human BAZ2B in complex with acetylated lysine
Structural highlights
FunctionBAZ2B_HUMAN May play a role in transcriptional regulation interacting with ISWI. Publication Abstract from PubMedBromodomains are epigenetic reader domains that have recently become popular targets. In contrast to BET bromodomains, which have proven druggable, bromodomains from other regions of the phylogenetic tree have shallower pockets. We describe successful targeting of the challenging BAZ2B bromodomain using biophysical fragment screening and structure-based optimization of high ligand-efficiency fragments into a novel series of low-micromolar inhibitors. Our results provide attractive leads for development of BAZ2B chemical probes and indicate the whole family may be tractable. Targeting low-druggability bromodomains: fragment based screening and inhibitor design against the BAZ2B bromodomain.,Ferguson FM, Fedorov O, Chaikuad A, Philpott M, Muniz JR, Felletar I, von Delft F, Heightman T, Knapp S, Abell C, Ciulli A J Med Chem. 2013 Dec 27;56(24):10183-7. doi: 10.1021/jm401582c. Epub 2013 Dec 13. PMID:24304323[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||