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2h9n

From Proteopedia

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{{Seed}}
 
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[[Image:2h9n.png|left|200px]]
 
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<!--
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==WDR5 in complex with monomethylated H3K4 peptide==
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The line below this paragraph, containing "STRUCTURE_2h9n", creates the "Structure Box" on the page.
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<StructureSection load='2h9n' size='340' side='right'caption='[[2h9n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[2h9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H9N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
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-->
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2h9l|2h9l]], [[2h9m|2h9m]], [[2h9o|2h9o]], [[2h9p|2h9p]]</div></td></tr>
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{{STRUCTURE_2h9n| PDB=2h9n | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDR5, BIG3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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=2h9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h9n OCA], [https://pdbe.org/2h9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h9n RCSB], [https://www.ebi.ac.uk/pdbsum/2h9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h9n 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> [[https://www.uniprot.org/uniprot/H33_XENTR H33_XENTR]] Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h9/2h9n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h9n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Histone methylation at specific lysine residues brings about various downstream events that are mediated by different effector proteins. The WD40 domain of WDR5 represents a new class of histone methyl-lysine recognition domains that is important for recruiting H3K4 methyltransferases to K4-dimethylated histone H3 tail as well as for global and gene-specific K4 trimethylation. Here we report the crystal structures of full-length WDR5, WDR5Delta23 and its complexes with unmodified, mono-, di- and trimethylated histone H3K4 peptides. The structures reveal that WDR5 is able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified lysine 4. We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes.
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===WDR5 in complex with monomethylated H3K4 peptide===
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Structural basis for molecular recognition and presentation of histone H3 by WDR5.,Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Arrowsmith CH, Min J EMBO J. 2006 Sep 20;25(18):4245-52. Epub 2006 Aug 31. PMID:16946699<ref>PMID:16946699</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 2h9n" style="background-color:#fffaf0;"></div>
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<!--
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16946699}}, 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 16946699 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_16946699}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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2H9N is a [[Protein complex]] structure of sequences 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=2H9N OCA].
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[[Category: Large Structures]]
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[[Category: Allali-Hassani, A]]
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==Reference==
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[[Category: Arrowsmith, C H]]
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Structural basis for molecular recognition and presentation of histone H3 by WDR5., Schuetz A, Allali-Hassani A, Martin F, Loppnau P, Vedadi M, Bochkarev A, Plotnikov AN, Arrowsmith CH, Min J, EMBO J. 2006 Sep 20;25(18):4245-52. Epub 2006 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16946699 16946699]
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[[Category: Bochkarev, A]]
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[[Category: Homo sapiens]]
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[[Category: Edwards, A M]]
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[[Category: Protein complex]]
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[[Category: Loppnau, P]]
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[[Category: Allali-Hassani, A.]]
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[[Category: Martin, F]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Min, J R]]
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[[Category: Bochkarev, A.]]
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[[Category: Plotnikov, A N]]
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[[Category: Edwards, A M.]]
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[[Category: Structural genomic]]
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[[Category: Loppnau, P.]]
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[[Category: Schuetz, A]]
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[[Category: Martin, F.]]
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[[Category: Sundstrom, M]]
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[[Category: Min, J R.]]
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[[Category: Vedadi, M]]
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[[Category: Plotnikov, A N.]]
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[[Category: Weigelt, J]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Gene regulation]]
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[[Category: Schuetz, A.]]
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[[Category: Sundstrom, M.]]
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[[Category: Vedadi, M.]]
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[[Category: Weigelt, J.]]
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[[Category: Sgc]]
[[Category: Sgc]]
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[[Category: Structural genomic]]
 
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[[Category: Structural genomics consortium]]
 
[[Category: Wdr5]]
[[Category: Wdr5]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:29:27 2008''
 

Current revision

WDR5 in complex with monomethylated H3K4 peptide

PDB ID 2h9n

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