5ewc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5ewc" [edit=sysop:move=sysop])
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: Caflisch, A]]
[[Category: Zhu, J]]
[[Category: Zhu, J]]
 +
[[Category: Dna binding protein]]
 +
[[Category: Inhibitor]]
 +
[[Category: Transcription]]

Revision as of 22:56, 1 June 2016

Crystal structure of the human BRPF1 bromodomain in complex with SEED17

5ewc, resolution 1.75Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ewc"
Personal tools