5ewc: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5ewc is ~~ON HOLD~~ ~~until Paper~~ Publication

==Crystal structure of the human BRPF1 bromodomain in complex with SEED17==

== Structural highlights ==

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

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5SJ:ETHYL+(2~{R})-2-METHYL-3-OXIDANYLIDENE-2,4-DIHYDRO-1~{H}-QUINOXALINE-6-CARBOXYLATE'>5SJ</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='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=5ewc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewc OCA], [http://pdbe.org/5ewc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ewc RCSB], [http://www.ebi.ac.uk/pdbsum/5ewc 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.

~~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 SEED17~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[Category~~: ~~Unreleased Structures]]~~

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Caflisch, A]]

[[Category: Zhu, J]]

[[Category: Dna binding protein]]

[[Category: Inhibitor]]

[[Category: Transcription]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ewc is ON HOLD  until Paper Publication
+==Crystal structure of the human BRPF1 bromodomain in complex with SEED17==
+<StructureSection load='5ewc' size='340' side='right' caption='[[5ewc]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ewc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EWC FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5SJ:ETHYL+(2~{R})-2-METHYL-3-OXIDANYLIDENE-2,4-DIHYDRO-1~{H}-QUINOXALINE-6-CARBOXYLATE'>5SJ</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='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=5ewc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewc OCA], [http://pdbe.org/5ewc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ewc RCSB], [http://www.ebi.ac.uk/pdbsum/5ewc 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.
-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 SEED17
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ewc" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Caflisch, A]]
 [[Category: Zhu, J]]
+[[Category: Dna binding protein]]
+[[Category: Inhibitor]]
+[[Category: Transcription]]