6e23

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'''Unreleased structure'''
 
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The entry 6e23 is ON HOLD until Paper Publication
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==Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with picomolar affinity==
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<StructureSection load='6e23' size='340' side='right'caption='[[6e23]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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Authors: Phan, J., Fesik, S.W.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6e23]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E23 FirstGlance]. <br>
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Description: Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with picomolar affinity
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HLJ:N-[(3,4-dichlorophenyl)methyl]-3-(6-fluoro-2-methylpyridin-3-yl)-5-{[(2E)-2-imino-3-methyl-2,3-dihydro-1H-imidazol-1-yl]methyl}benzamide'>HLJ</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6d9x|6d9x]]</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=6e23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e23 OCA], [http://pdbe.org/6e23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e23 RCSB], [http://www.ebi.ac.uk/pdbsum/6e23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e23 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
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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: Large Structures]]
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[[Category: Fesik, S W]]
[[Category: Phan, J]]
[[Category: Phan, J]]
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[[Category: Fesik, S.W]]
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[[Category: Dna binding protein]]
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[[Category: Dna binding protein-inhibitor complex]]
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[[Category: Fragment screening]]
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[[Category: Gene regulation]]
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[[Category: Gene regulation-inhibitor complex]]
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[[Category: Mixed-lineage leukemia]]
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[[Category: Structure-based design]]
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[[Category: Wdr5]]
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[[Category: Win-site]]

Revision as of 11:56, 13 March 2019

Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with picomolar affinity

PDB ID 6e23

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