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7axx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of WDR5:CS-VIP8 crystal after illumination at 405 nm and room temperature== | |
| + | <StructureSection load='7axx' size='340' side='right'caption='[[7axx]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7axx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AXX FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4FO:(2R)-2,4-DIAMINOBUTANOIC+ACID'>4FO</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=EDN:ETHANE-1,2-DIAMINE'>EDN</scene>, <scene name='pdbligand=S7Z:(E)-(4-((2,6-difluoro-4-(hydroxymethyl)phenyl)diazenyl)-2,6-difluorophenyl)methanol'>S7Z</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7axx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7axx OCA], [https://pdbe.org/7axx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7axx RCSB], [https://www.ebi.ac.uk/pdbsum/7axx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7axx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | ||
| - | + | ==See Also== | |
| - | + | *[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Essen | + | __TOC__ |
| - | [[Category: Werel | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Essen L-O]] | ||
| + | [[Category: Werel L]] | ||
Current revision
Structure of WDR5:CS-VIP8 crystal after illumination at 405 nm and room temperature
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