6dar: Difference between revisions

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-'''Unreleased structure'''
-The entry 6dar is ON HOLD  until Paper Publication
+==Discovery of Potent 2-Aryl-6,7-Dihydro-5HPyrrolo[ 1,2-a]imidazoles as WDR5 WIN-site Inhibitors Using Fragment-Based Methods and Structure-Based Design==
+<StructureSection load='6dar' size='340' side='right' caption='[[6dar]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
-Authors: Phan, J., Fesik, S.W.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6dar]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DAR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DAR FirstGlance]. <br>
-Description: Discovery of Potent 2-Aryl-6,7-Dihydro-5HPyrrolo[ 1,2-a]imidazoles as WDR5 WIN-site Inhibitors Using Fragment-Based Methods and Structure-Based Design
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=G2J:N-(cyclopropylmethyl)-N-{[3-(6,7-dihydro-5H-pyrrolo[1,2-a]imidazol-2-yl)phenyl]methyl}-3-methoxybenzamide'>G2J</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=6dar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dar OCA], [http://pdbe.org/6dar PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dar RCSB], [http://www.ebi.ac.uk/pdbsum/6dar PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dar ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Fesik, S W]]
 [[Category: Phan, J]]
-[[Category: Fesik, S.W]]
+[[Category: Dna binding protein]]
+[[Category: Dna binding protein-inhibitor complex]]
+[[Category: Fragment screening]]
+[[Category: Mixed-lineage leukemia]]
+[[Category: Structure-based design]]
+[[Category: Wdr5]]
+[[Category: Win-site]]