4a7j

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[[Image:4a7j.png|left|200px]]
 
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==Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin Maintenance==
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The line below this paragraph, containing "STRUCTURE_4a7j", creates the "Structure Box" on the page.
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<StructureSection load='4a7j' size='340' side='right'caption='[[4a7j]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4a7j]] 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=4A7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A7J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MR:N3,+N4-DIMETHYLARGININE'>2MR</scene></td></tr>
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{{STRUCTURE_4a7j| PDB=4a7j | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a7j OCA], [https://pdbe.org/4a7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a7j RCSB], [https://www.ebi.ac.uk/pdbsum/4a7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a7j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The asymmetric dimethylation of histone H3 arginine 2 (H3R2me2a) acts as a repressive mark that antagonizes trimethylation of H3 lysine 4. Here we report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions. Profiling of H3-tail interactors by SILAC MS revealed that H3R2me2s excludes binding of RBBP7, a central component of co-repressor complexes Sin3a, NURD and PRC2. Conversely H3R2me2s enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC. The interaction of histone H3 with WDR5 distinguishes H3R2me2s from H3R2me2a, which impedes the recruitment of WDR5 to chromatin. The crystallographic structure of WDR5 and the H3R2me2s peptide elucidates the molecular determinants of this high affinity interaction. Our findings identify H3R2me2s as a previously unknown mark that keeps genes poised in euchromatin for transcriptional activation upon cell-cycle withdrawal and differentiation in human cells.
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===Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin Maintenance===
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Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance.,Migliori V, Muller J, Phalke S, Low D, Bezzi M, Mok WC, Sahu SK, Gunaratne J, Capasso P, Bassi C, Cecatiello V, De Marco A, Blackstock W, Kuznetsov V, Amati B, Mapelli M, Guccione E Nat Struct Mol Biol. 2012 Jan 8;19(2):136-44. doi: 10.1038/nsmb.2209. PMID:22231400<ref>PMID:22231400</ref>
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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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<div class="pdbe-citations 4a7j" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22231400}}, adds the Publication Abstract to the page
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*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22231400 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22231400}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[4a7j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A7J OCA].
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==Reference==
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<ref group="xtra">PMID:022231400</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Amati, B.]]
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[[Category: Large Structures]]
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[[Category: Bassi, C.]]
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[[Category: Amati B]]
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[[Category: Bezzi, M.]]
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[[Category: Bassi C]]
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[[Category: Blackstock, W.]]
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[[Category: Bezzi M]]
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[[Category: Capasso, P.]]
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[[Category: Blackstock W]]
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[[Category: Cecatiello, V.]]
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[[Category: Capasso P]]
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[[Category: Chuenmok, W.]]
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[[Category: Cecatiello V]]
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[[Category: Demarco, A.]]
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[[Category: ChuenMok W]]
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[[Category: Guccione, E.]]
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[[Category: DeMarco A]]
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[[Category: Gunaratne, J.]]
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[[Category: Guccione E]]
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[[Category: Kuznetsov, V.]]
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[[Category: Gunaratne J]]
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[[Category: Low, D.]]
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[[Category: Kuznetsov V]]
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[[Category: Mapelli, M.]]
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[[Category: Low D]]
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[[Category: Migliori, V.]]
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[[Category: Mapelli M]]
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[[Category: Muller, J.]]
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[[Category: Migliori V]]
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[[Category: Phalke, S.]]
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[[Category: Muller J]]
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[[Category: Histone methylation]]
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[[Category: Phalke S]]
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[[Category: Transcription]]
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Current revision

Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin Maintenance

PDB ID 4a7j

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