2pqw

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[[Image:2pqw.jpg|left|200px]]
 
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==Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form==
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The line below this paragraph, containing "STRUCTURE_2pqw", creates the "Structure Box" on the page.
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<StructureSection load='2pqw' size='340' side='right'caption='[[2pqw]], [[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'>[[2pqw]] 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=2PQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQW FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
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{{STRUCTURE_2pqw| PDB=2pqw | 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=2pqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqw OCA], [https://pdbe.org/2pqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqw RCSB], [https://www.ebi.ac.uk/pdbsum/2pqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqw ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form'''
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== Function ==
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[https://www.uniprot.org/uniprot/LMBL1_HUMAN LMBL1_HUMAN] Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis.<ref>PMID:17540172</ref> <ref>PMID:18408754</ref> <ref>PMID:20870719</ref> <ref>PMID:20870725</ref>
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== Evolutionary Conservation ==
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==Overview==
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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/pq/2pqw_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=2pqw 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 ==
Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.
Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.
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==About this Structure==
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L3MBTL1 recognition of mono- and dimethylated histones.,Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18. PMID:18026117<ref>PMID:18026117</ref>
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2PQW is a [[Single protein]] structure of 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=2PQW OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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L3MBTL1 recognition of mono- and dimethylated histones., Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH, Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18026117 18026117]
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</div>
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<div class="pdbe-citations 2pqw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Allali-Hassani, A.]]
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[[Category: Allali-Hassani A]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Bochkarev, A.]]
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[[Category: Bochkarev A]]
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[[Category: Crombet, L.]]
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[[Category: Crombet L]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Herzanych, N.]]
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[[Category: Herzanych N]]
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[[Category: Kozieradzki, I.]]
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[[Category: Kozieradzki I]]
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[[Category: Liu, Y.]]
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[[Category: Liu Y]]
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[[Category: Loppnau, P.]]
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[[Category: Loppnau P]]
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[[Category: Mackenzie, F.]]
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[[Category: Mackenzie F]]
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[[Category: Min, J R.]]
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[[Category: Min JR]]
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[[Category: Ouyang, H.]]
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[[Category: Ouyang H]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M.]]
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[[Category: Vedadi M]]
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[[Category: Vedadi, M.]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J.]]
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[[Category: Sgc]]
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[[Category: Structural genomic]]
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[[Category: Structural genomics consortium]]
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[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:39:08 2008''
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Current revision

Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form

PDB ID 2pqw

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