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2w5z
From Proteopedia
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| - | {{STRUCTURE_2w5z| PDB=2w5z | SCENE= }} | ||
| - | ===TERNARY COMPLEX OF THE MIXED LINEAGE LEUKAEMIA (MLL1) SET DOMAIN WITH THE COFACTOR PRODUCT S-ADENOSYLHOMOCYSTEINE AND HISTONE PEPTIDE.=== | ||
| - | {{ABSTRACT_PUBMED_19187761}} | ||
| - | == | + | ==Ternary Complex of the Mixed Lineage Leukaemia (MLL1) SET Domain with the cofactor product S-Adenosylhomocysteine and histone peptide.== |
| - | [[2w5z]] is a 2 chain structure with sequence from [ | + | <StructureSection load='2w5z' size='340' side='right'caption='[[2w5z]], [[Resolution|resolution]] 2.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2w5z]] is a 2 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=2W5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W5Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2agh|2agh]], [[2j2s|2j2s]], [[2w5y|2w5y]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></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=2w5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w5z OCA], [https://pdbe.org/2w5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w5z RCSB], [https://www.ebi.ac.uk/pdbsum/2w5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w5z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/2w5z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2w5z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mixed-lineage leukemia protein MLL1 is a transcriptional regulator with an essential role in early development and hematopoiesis. The biological function of MLL1 is mediated by the histone H3K4 methyltransferase activity of the carboxyl-terminal SET domain. We have determined the crystal structure of the MLL1 SET domain in complex with cofactor product AdoHcy and a histone H3 peptide. This structure indicates that, in order to form a well-ordered active site, a highly variable but essential component of the SET domain must be repositioned. To test this idea, we compared the effect of the addition of MLL complex members on methyltransferase activity and show that both RbBP5 and Ash2L but not Wdr5 stimulate activity. Additionally, we have determined the effect of posttranslational modifications on histone H3 residues downstream and upstream from the target lysine and provide a structural explanation for why H3T3 phosphorylation and H3K9 acetylation regulate activity. | ||
| - | + | Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks.,Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR Mol Cell. 2009 Jan 30;33(2):181-91. PMID:19187761<ref>PMID:19187761</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2w5z" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: Odho, Z | + | [[Category: Large Structures]] |
| - | [[Category: Roe, S M | + | [[Category: Odho, Z]] |
| - | [[Category: Southall, S M | + | [[Category: Roe, S M]] |
| - | [[Category: Wilson, J R | + | [[Category: Southall, S M]] |
| - | [[Category: Wong, P S | + | [[Category: Wilson, J R]] |
| + | [[Category: Wong, P S]] | ||
| + | [[Category: Alternative splicing]] | ||
[[Category: Apoptosis]] | [[Category: Apoptosis]] | ||
[[Category: Bromodomain]] | [[Category: Bromodomain]] | ||
[[Category: Chromatin regulator]] | [[Category: Chromatin regulator]] | ||
| + | [[Category: Chromosomal rearrangement]] | ||
[[Category: Dna-binding]] | [[Category: Dna-binding]] | ||
[[Category: Histone modification]] | [[Category: Histone modification]] | ||
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[[Category: Nucleus]] | [[Category: Nucleus]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
| + | [[Category: Polymorphism]] | ||
[[Category: Protein lysine methyltransferase]] | [[Category: Protein lysine methyltransferase]] | ||
[[Category: Proto-oncogene]] | [[Category: Proto-oncogene]] | ||
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[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
| + | [[Category: Ubl conjugation]] | ||
| + | [[Category: Zinc]] | ||
[[Category: Zinc-finger]] | [[Category: Zinc-finger]] | ||
Current revision
Ternary Complex of the Mixed Lineage Leukaemia (MLL1) SET Domain with the cofactor product S-Adenosylhomocysteine and histone peptide.
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Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Odho, Z | Roe, S M | Southall, S M | Wilson, J R | Wong, P S | Alternative splicing | Apoptosis | Bromodomain | Chromatin regulator | Chromosomal rearrangement | Dna-binding | Histone modification | Kmt2a | Metal-binding | Methyltransferase | Mixed lineage leukaemia | Mll1 | Nucleus | Phosphoprotein | Polymorphism | Protein lysine methyltransferase | Proto-oncogene | S-adenosyl-l-methionine | Set domain | Transcription | Transcription regulation | Transferase | Ubl conjugation | Zinc | Zinc-finger
