5eva

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'''Unreleased structure'''
 
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The entry 5eva is ON HOLD
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==Crystal structure of the human BRPF1 bromodomain in complex with SEED16==
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<StructureSection load='5eva' size='340' side='right'caption='[[5eva]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5eva]] 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=5EVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EVA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5S9:~{N}-[2,4-BIS(FLUORANYL)PHENYL]-2-METHYL-PYRAZOLE-3-CARBOXAMIDE'>5S9</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5eva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eva OCA], [https://pdbe.org/5eva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eva RCSB], [https://www.ebi.ac.uk/pdbsum/5eva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eva ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Zhu, J., Caflisch, A.
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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>
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Description: Crystal structure of the human BRPF1 bromodomain in complex with SEED16
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Caflisch, A]]
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<div class="pdbe-citations 5eva" style="background-color:#fffaf0;"></div>
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[[Category: Zhu, J]]
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==See Also==
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*[[Peregrin|Peregrin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Caflisch A]]
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[[Category: Zhu J]]

Current revision

Crystal structure of the human BRPF1 bromodomain in complex with SEED16

PDB ID 5eva

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