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| - | [[Image:3uvm.png|left|200px]] | |
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| - | <!--
| + | ==Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4== |
| - | The line below this paragraph, containing "STRUCTURE_3uvm", creates the "Structure Box" on the page.
| + | <StructureSection load='3uvm' size='340' side='right'caption='[[3uvm]], [[Resolution|resolution]] 1.57Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3uvm]] 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=3UVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UVM FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57Å</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=3uvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uvm OCA], [https://pdbe.org/3uvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uvm RCSB], [https://www.ebi.ac.uk/pdbsum/3uvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uvm ProSAT]</span></td></tr> |
| - | {{STRUCTURE_3uvm| PDB=3uvm | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [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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| - | ===Crystal structure of WDR5 in complex with the WDR5-interacting motif of MLL4=== | + | ==See Also== |
| - | | + | *[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]] |
| - | | + | == References == |
| - | <!--
| + | <references/> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_22266653}}, adds the Publication Abstract to the page
| + | __TOC__ |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 22266653 is the PubMed ID number.
| + | </StructureSection> |
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| + | |
| - | {{ABSTRACT_PUBMED_22266653}}
| + | |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | [[3uvm]] 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=3UVM OCA].
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| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:022266653</ref><references group="xtra"/> | + | |
| - | [[Category: Histone-lysine N-methyltransferase]]
| + | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Brunzelle, J S.]] | + | [[Category: Large Structures]] |
| - | [[Category: Couture, J F.]] | + | [[Category: Brunzelle JS]] |
| - | [[Category: Lee, H.]] | + | [[Category: Couture J-F]] |
| - | [[Category: Zhang, P.]] | + | [[Category: Lee H]] |
| - | [[Category: Beta-propeller]]
| + | [[Category: Zhang P]] |
| - | [[Category: Chromatin biology]]
| + | |
| - | [[Category: Histone h3]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Scaffolding]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Trithorax]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
See Also
References
- ↑ Patel A, Dharmarajan V, Vought VE, Cosgrove MS. On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. PMID:19556245 doi:M109.014498
- ↑ Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, Wu J, Lill JR, Zha J. The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol Cell Biol. 2009 Mar;29(5):1176-88. doi: 10.1128/MCB.01599-08. Epub 2008 Dec, 22. PMID:19103755 doi:10.1128/MCB.01599-08
- ↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
- ↑ Han Z, Guo L, Wang H, Shen Y, Deng XW, Chai J. Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Mol Cell. 2006 Apr 7;22(1):137-44. PMID:16600877 doi:10.1016/j.molcel.2006.03.018
- ↑ Couture JF, Collazo E, Trievel RC. Molecular recognition of histone H3 by the WD40 protein WDR5. Nat Struct Mol Biol. 2006 Aug;13(8):698-703. Epub 2006 Jul 9. PMID:16829960 doi:10.1038/nsmb1116
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