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| | <StructureSection load='4cy5' size='340' side='right'caption='[[4cy5]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4cy5' size='340' side='right'caption='[[4cy5]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cy5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CY5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cy5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CY5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cy1|4cy1]], [[4cy2|4cy2]], [[4cy3|4cy3]]</td></tr> | + | </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=4cy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy5 OCA], [https://pdbe.org/4cy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cy5 RCSB], [https://www.ebi.ac.uk/pdbsum/4cy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy5 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></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=4cy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy5 OCA], [http://pdbe.org/4cy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cy5 RCSB], [http://www.ebi.ac.uk/pdbsum/4cy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/WDS_DROME WDS_DROME]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). | + | [[https://www.uniprot.org/uniprot/WDS_DROME WDS_DROME]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Inorganic diphosphatase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brettschneider, J]] | + | [[Category: Brettschneider J]] |
| - | [[Category: Cusack, S]] | + | [[Category: Cusack S]] |
| - | [[Category: Dias, J]] | + | [[Category: Dias J]] |
| - | [[Category: Kadlec, J]] | + | [[Category: Kadlec J]] |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Epigenetic regulator]]
| + | |
| - | [[Category: Histone acetylation]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
[WDS_DROME] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity).
Publication Abstract from PubMed
The subunits of the nonspecific lethal (NSL) complex, which include the histone acetyltransferase MOF (males absent on the first), play important roles in various cellular functions, including transcription regulation and stem cell identity maintenance and reprogramming, and are frequently misregulated in disease. Here, we provide the first biochemical and structural insights into the molecular architecture of this large multiprotein assembly. We identified several direct interactions within the complex and show that KANSL1 acts as a scaffold protein interacting with four other subunits, including WDR5, which in turn binds KANSL2. Structural analysis of the KANSL1/WDR5/KANSL2 subcomplex reveals how WDR5 is recruited into the NSL complex via conserved linear motifs of KANSL1 and KANSL2. Using structure-based KANSL1 mutants in transgenic flies, we show that the KANSL1-WDR5 interaction is required for proper assembly, efficient recruitment of the NSL complex to target promoters, and fly viability. Our data clearly show that the interactions of WDR5 with the MOF-containing NSL complex and MLL/COMPASS histone methyltransferase complexes are mutually exclusive. We propose that rather than being a shared subunit, WDR5 plays an important role in assembling distinct histone-modifying complexes with different epigenetic regulatory roles.
Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex.,Dias J, Van Nguyen N, Georgiev P, Gaub A, Brettschneider J, Cusack S, Kadlec J, Akhtar A Genes Dev. 2014 May 1;28(9):929-42. doi: 10.1101/gad.240200.114. PMID:24788516[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dias J, Van Nguyen N, Georgiev P, Gaub A, Brettschneider J, Cusack S, Kadlec J, Akhtar A. Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex. Genes Dev. 2014 May 1;28(9):929-42. doi: 10.1101/gad.240200.114. PMID:24788516 doi:http://dx.doi.org/10.1101/gad.240200.114
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