4riq

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'''Unreleased structure'''
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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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<StructureSection load='4riq' size='340' side='right' caption='[[4riq]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4riq is ON HOLD until Paper Publication
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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>
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Authors: Tremblay, V., Couture, J.-F.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of DPY-30 dimerization/docking domain in complex with Ash2L Sdc1-DPY-30 Interacting region (SDI)
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Couture, J F]]
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[[Category: Tremblay, V]]
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[[Category: Allosteric regulator]]
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[[Category: Ash2l]]
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[[Category: Chromatin]]
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[[Category: Dimerization/docking module]]
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[[Category: Histone]]
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[[Category: Methylation]]
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[[Category: Mll1]]
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[[Category: Mll2]]
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[[Category: Mll3]]
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[[Category: Mll4]]
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[[Category: Rbbp5]]
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[[Category: Set1a]]
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[[Category: Set1b]]
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[[Category: Transferase-protein binding complex]]
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[[Category: Wdr5]]

Revision as of 12:37, 17 December 2014

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

4riq, resolution 2.23Å

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