6e22: Difference between revisions

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-'''Unreleased structure'''
-The entry 6e22 is ON HOLD  until Paper Publication
+==Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with picomolar affinity==
+<StructureSection load='6e22' size='340' side='right'caption='[[6e22]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-Authors: Phan, J., Fesik, S.W.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6e22]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E22 FirstGlance]. <br>
-Description: Displacement of WDR5 from chromatin by a pharmacological WIN site inhibitor with picomolar affinity
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLS:3-{[(4,5-dihydro-1H-imidazol-2-yl)amino]methyl}-N-[(3,5-dimethoxyphenyl)methyl]-4-fluorobenzamide'>HLS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6d9x|6d9x]]</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=6e22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e22 OCA], [http://pdbe.org/6e22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e22 RCSB], [http://www.ebi.ac.uk/pdbsum/6e22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e22 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: Large Structures]]
+[[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: Gene regulation]]
+[[Category: Gene regulation-inhibitor complex]]
+[[Category: Mixed-lineage leukemia]]
+[[Category: Structure-based design]]
+[[Category: Wdr5]]
+[[Category: Win-site]]