2pqw

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[[Image:2pqw.jpg|left|200px]]<br /><applet load="2pqw" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pqw, resolution 2.00&Aring;" />
 
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'''Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form'''<br />
 
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==Overview==
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==Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form==
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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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<StructureSection load='2pqw' size='340' side='right'caption='[[2pqw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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== 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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[[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 ==
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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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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 Nov 18;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: ACT]]
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[[Category: l(3)mbt-like protein]]
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[[Category: sgc]]
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[[Category: structural genomics]]
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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 Wed Jan 23 11:31:27 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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