4cy3
From Proteopedia
(Difference between revisions)
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<StructureSection load='4cy3' size='340' side='right' caption='[[4cy3]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4cy3' size='340' side='right' caption='[[4cy3]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4cy3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY3 OCA]. <br> | + | <table><tr><td colspan='2'>[[4cy3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CY3 FirstGlance]. <br> |
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cy1|4cy1]], [[4cy2|4cy2]], [[4cy5|4cy5]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cy1|4cy1]], [[4cy2|4cy2]], [[4cy5|4cy5]]</td></tr> |
- | <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=4cy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cy3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cy3 PDBsum]</span></td></tr> |
- | + | </table> | |
- | <table> | + | == 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). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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<ref>PMID:24788516</ref> | 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<ref>PMID:24788516</ref> | ||
- | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[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: Chromatin]] | ||
[[Category: Epigenetic regulator]] | [[Category: Epigenetic regulator]] | ||
[[Category: Histone acetylation]] | [[Category: Histone acetylation]] | ||
[[Category: Transcription]] | [[Category: Transcription]] |
Revision as of 16:32, 25 December 2014
Crystal structure of the NSL1-WDS complex.
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