4j1p
From Proteopedia
(Difference between revisions)
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| - | + | ==X-ray crystal structure of bromodomain 2 of human brd2 in complex with rvx208 to 1.08 A resolution== | |
| - | + | <StructureSection load='4j1p' size='340' side='right' caption='[[4j1p]], [[Resolution|resolution]] 1.08Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4j1p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J1P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1K0:2-[4-(2-HYDROXYETHOXY)-3,5-DIMETHYLPHENYL]-5,7-DIMETHOXYQUINAZOLIN-4(3H)-ONE'>1K0</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j3i|4j3i]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BRD2, DKFZp313H139, hCG_17503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4j1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j1p RCSB], [http://www.ebi.ac.uk/pdbsum/4j1p PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Increased synthesis of Apolipoprotein A-I (ApoA-I) and HDL is believed to provide a new approach to treating atherosclerosis through the stimulation of reverse cholesterol transport. RVX-208 increases the production of ApoA-I in hepatocytes in vitro, and in vivo in monkeys and humans, which results in increased HDL-C, but the molecular target was not previously reported. Using binding assays and X-ray crystallography, we now show that RVX-208 selectively binds to bromodomains of the BET (Bromodomain and Extra Terminal) family, competing for a site bound by the endogenous ligand, acetylated lysine, and that this accounts for its pharmacological activity. siRNA experiments further suggest that induction of ApoA-I mRNA is mediated by BET family member BRD4. These data indicate that RVX-208 increases ApoA-I production through an epigenetic mechanism and suggests that BET inhibition may be a promising new approach to the treatment of atherosclerosis. | ||
| - | + | RVX-208, an Inducer of ApoA-I in Humans, Is a BET Bromodomain Antagonist.,McLure KG, Gesner EM, Tsujikawa L, Kharenko OA, Attwell S, Campeau E, Wasiak S, Stein A, White A, Fontano E, Suto RK, Wong NC, Wagner GS, Hansen HC, Young PR PLoS One. 2013 Dec 31;8(12):e83190. doi: 10.1371/journal.pone.0083190. PMID:24391744<ref>PMID:24391744</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Stein, A J | + | == References == |
| - | [[Category: Suto, R K | + | <references/> |
| - | [[Category: White, A | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Stein, A J]] | ||
| + | [[Category: Suto, R K]] | ||
| + | [[Category: White, A]] | ||
[[Category: Brd2]] | [[Category: Brd2]] | ||
[[Category: Bromodomain]] | [[Category: Bromodomain]] | ||
[[Category: Signaling protein-inhibitor complex]] | [[Category: Signaling protein-inhibitor complex]] | ||
Revision as of 09:50, 20 January 2015
X-ray crystal structure of bromodomain 2 of human brd2 in complex with rvx208 to 1.08 A resolution
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