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4riq

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Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)

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Categories: Homo sapiens | Large Structures | Couture J-F | Tremblay V

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 ==Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)==
-<StructureSection load='4riq' size='340' side='right' caption='[[4riq]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
+<StructureSection load='4riq' size='340' side='right'caption='[[4riq]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4riq]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RIQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4riq]] is a 24 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=4RIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RIQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.231&#8491;</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=4riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4riq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4riq RCSB], [http://www.ebi.ac.uk/pdbsum/4riq PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4riq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4riq OCA], [https://pdbe.org/4riq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4riq RCSB], [https://www.ebi.ac.uk/pdbsum/4riq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4riq ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/DPY30_HUMAN DPY30_HUMAN] As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.<ref>PMID:19556245</ref> <ref>PMID:19651892</ref> <ref>PMID:21335234</ref>
-DPY-30 is a subunit of mammalian COMPASS-like complexes (complex of proteins associated with Set1) and regulates global histone H3 Lys-4 trimethylation. Here we report structural evidence showing that the incorporation of DPY-30 into COMPASS-like complexes is mediated by several hydrophobic interactions between an amphipathic alpha helix located on the C terminus of COMPASS subunit ASH2L and the inner surface of the DPY-30 dimerization/docking (D/D) module. Mutations impairing the interaction between ASH2L and DPY-30 result in a loss of histone H3K4me3 at the beta locus control region and cause a delay in erythroid cell terminal differentiation. Using overlay assays, we defined a consensus sequence for DPY-30 binding proteins and found that DPY-30 interacts with BAP18, a subunit of the nucleosome remodeling factor complex. Overall, our results indicate that the ASH2L/DPY-30 complex is important for cell differentiation and provide insights into the ability of DPY-30 to associate with functionally divergent multisubunit complexes.
-Molecular Basis for DPY-30 Association to COMPASS-like and NURF Complexes.,Tremblay V, Zhang P, Chaturvedi CP, Thornton J, Brunzelle JS, Skiniotis G, Shilatifard A, Brand M, Couture JF Structure. 2014 Dec 2;22(12):1821-30. doi: 10.1016/j.str.2014.10.002. Epub 2014, Nov 20. PMID:25456412<ref>PMID:25456412</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Couture, J F]]
+[[Category: Homo sapiens]]
-[[Category: Tremblay, V]]
+[[Category: Large Structures]]
-[[Category: Allosteric regulator]]
+[[Category: Couture J-F]]
-[[Category: Ash2l]]
+[[Category: Tremblay V]]
-[[Category: Chromatin]]
-[[Category: Dimerization/docking module]]
-[[Category: Histone]]
-[[Category: Methylation]]
-[[Category: Mll1]]
-[[Category: Mll2]]
-[[Category: Mll3]]
-[[Category: Mll4]]
-[[Category: Rbbp5]]
-[[Category: Set1a]]
-[[Category: Set1b]]
-[[Category: Transferase-protein binding complex]]
-[[Category: Wdr5]]

4riq

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Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)

Structural highlights

Function

See Also

References

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