5e3g

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'''Unreleased structure'''
 
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The entry 5e3g is ON HOLD until Paper Publication
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==Crystal structure of the human BRPF1 bromodomain in complex with SEED8==
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<StructureSection load='5e3g' size='340' side='right' caption='[[5e3g]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5e3g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E3G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5JQ:2-THIOXO-2,3,7,9-TETRAHYDRO-1H-PURINE-6,8-DIONE'>5JQ</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c7n|5c7n]], [[5c85|5c85]], [[5c87|5c87]], [[5c89|5c89]], [[5d7x|5d7x]], [[5dya|5dya]], [[5dy7|5dy7]], [[5dyc|5dyc]], [[5e3d|5e3d]]</td></tr>
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<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=5e3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e3g OCA], [http://pdbe.org/5e3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e3g RCSB], [http://www.ebi.ac.uk/pdbsum/5e3g PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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>
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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 SEED8
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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: Zhu, J]]
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<div class="pdbe-citations 5e3g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Caflisch, A]]
[[Category: Caflisch, A]]
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[[Category: Zhu, J]]
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[[Category: Dna binding protein]]
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[[Category: Inhibitor]]
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[[Category: Transcription]]

Revision as of 22:55, 1 June 2016

Crystal structure of the human BRPF1 bromodomain in complex with SEED8

5e3g, resolution 1.65Å

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