5c85: Difference between revisions

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-'''Unreleased structure'''
-The entry 5c85 is ON HOLD  until Paper Publication
+==Crystal structure of the human BRPF1 bromodomain in complex with SEED1==
+<StructureSection load='5c85' size='340' side='right'caption='[[5c85]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5c85]] 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=5C85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C85 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c85 OCA], [https://pdbe.org/5c85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c85 RCSB], [https://www.ebi.ac.uk/pdbsum/5c85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c85 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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.
-Authors: Zhu, J., Caflisch, A.
+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>
-Description: Crystal structure of the human BRPF1 bromodomain in complex with SEED1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Caflisch, A]]
+<div class="pdbe-citations 5c85" style="background-color:#fffaf0;"></div>
-[[Category: Zhu, J]]
+==See Also==
+*[[Peregrin|Peregrin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Caflisch A]]
+[[Category: Zhu J]]