5ewc: Difference between revisions
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==Crystal structure of the human BRPF1 bromodomain in complex with SEED17== | |||
<StructureSection load='5ewc' size='340' side='right' caption='[[5ewc]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ewc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EWC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5SJ:ETHYL+(2~{R})-2-METHYL-3-OXIDANYLIDENE-2,4-DIHYDRO-1~{H}-QUINOXALINE-6-CARBOXYLATE'>5SJ</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c7n|5c7n]]</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=5ewc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewc OCA], [http://pdbe.org/5ewc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ewc RCSB], [http://www.ebi.ac.uk/pdbsum/5ewc PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/BRPF1_HUMAN BRPF1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.<ref>PMID:16387653</ref> <ref>PMID:18794358</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BRPF1 plays a scaffolding role in transcription. We report on fragment screening by high-throughput docking to the BRPF1 bromodomain which resulted in six chemotypes with very favorable ligand efficiency (0.45-0.50 kcal/mol per non-hydrogen atom). Twenty crystal structures of BRPF1/ligand complexes show structural conservation in the acetyllysine binding site, common binding motifs, and unusual interactions (e.g., the replacement of a conserved water molecule). The structural information is useful for the design of chemical probes. | |||
Twenty Crystal Structures of Bromodomain and PHD Finger Containing Protein 1 (BRPF1)/Ligand Complexes Reveal Conserved Binding Motifs and Rare Interactions.,Zhu J, Caflisch A J Med Chem. 2016 May 24. PMID:27167503<ref>PMID:27167503</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ewc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caflisch, A]] | [[Category: Caflisch, A]] | ||
[[Category: Zhu, J]] | [[Category: Zhu, J]] | ||
[[Category: Dna binding protein]] | |||
[[Category: Inhibitor]] | |||
[[Category: Transcription]] | |||
Revision as of 22:56, 1 June 2016
Crystal structure of the human BRPF1 bromodomain in complex with SEED17
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