5c7n: Difference between revisions

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==Crystal structure of the human BRPF1 bromodomain in complex with Bromosporine==

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<table><tr><td colspan='2'>[[5c7n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C7N FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMF:BROMOSPORINE'>BMF</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=5c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5c7n RCSB], [http://www.ebi.ac.uk/pdbsum/5c7n PDBsum]</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=5c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7n OCA], [http://pdbe.org/5c7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c7n RCSB], [http://www.ebi.ac.uk/pdbsum/5c7n 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>

== 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>

== References ==

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 ==Crystal structure of the human BRPF1 bromodomain in complex with Bromosporine==
 <StructureSection load='5c7n' size='340' side='right' caption='[[5c7n]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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 <table><tr><td colspan='2'>[[5c7n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C7N FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMF:BROMOSPORINE'>BMF</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=5c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5c7n RCSB], [http://www.ebi.ac.uk/pdbsum/5c7n PDBsum]</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=5c7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7n OCA], [http://pdbe.org/5c7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c7n RCSB], [http://www.ebi.ac.uk/pdbsum/5c7n 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5c7n" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>