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==Crystal structure of the human BRPF1 bromodomain in complex with SEED1== | ==Crystal structure of the human BRPF1 bromodomain in complex with SEED1== | ||
<StructureSection load='5c85' size='340' side='right' caption='[[5c85]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5c85' size='340' side='right'caption='[[5c85]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c85]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C85 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5c85]] 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=5C85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C85 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4YO:6-BROMO-3,4-DIHYDROQUINOXALIN-2(1H)-ONE'>4YO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4YO:6-BROMO-3,4-DIHYDROQUINOXALIN-2(1H)-ONE'>4YO</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c7n|5c7n]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRPF1, BR140 ([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=5c85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c85 OCA], [http://pdbe.org/5c85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c85 RCSB], [http://www.ebi.ac.uk/pdbsum/5c85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c85 ProSAT]</span></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=5c85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c85 OCA], [http://pdbe.org/5c85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c85 RCSB], [http://www.ebi.ac.uk/pdbsum/5c85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c85 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5c85" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5c85" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Peregrin|Peregrin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Caflisch, A]] | [[Category: Caflisch, A]] | ||
[[Category: Zhu, J]] | [[Category: Zhu, J]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 14:15, 18 March 2020
Crystal structure of the human BRPF1 bromodomain in complex with SEED1Crystal structure of the human BRPF1 bromodomain in complex with SEED1
Structural highlights
Function[BRPF1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Positively regulates the transcription of RUNX1 and RUNX2.[1] [2] Publication Abstract from PubMedBRPF1 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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