7m5u

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Current revision (16:05, 18 October 2023) (edit) (undo)
 
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==Crystal structure of human MPP8 chromodomain in complex with peptidomimetic ligand UNC5246==
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<StructureSection load='7m5u' size='340' side='right'caption='[[7m5u]]' scene=''>
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<StructureSection load='7m5u' size='340' side='right'caption='[[7m5u]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7m5u]] 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=7M5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M5U FirstGlance]. <br>
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</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=7m5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5u OCA], [https://pdbe.org/7m5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5u RCSB], [https://www.ebi.ac.uk/pdbsum/7m5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5u ProSAT]</span></td></tr>
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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]] 2.02&#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=5T3:N~6~-ethyl-N~6~-propan-2-yl-L-lysine'>5T3</scene>, <scene name='pdbligand=MN1:4-CARBOXYPIPERIDINE'>MN1</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</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=7m5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m5u OCA], [https://pdbe.org/7m5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m5u RCSB], [https://www.ebi.ac.uk/pdbsum/7m5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m5u ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MPP8_HUMAN MPP8_HUMAN] Involved in transcriptional regulation. Specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene. Mediates down-regulation of CDH1 expression.<ref>PMID:20871592</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The interpretation of histone post-translational modifications (PTMs), specifically lysine methylation, by specific classes of "reader" proteins marks an important aspect of epigenetic control of gene expression. Methyl-lysine (Kme) readers often regulate gene expression patterns through the recognition of a specific Kme PTM while participating in or recruiting large protein complexes that contain enzymatic or chromatin remodeling activity. Understanding the composition of these Kme-reader-containing protein complexes can serve to further our understanding of the biological roles of Kme readers, while small molecule chemical tools can be valuable reagents in interrogating novel protein-protein interactions. Here, we describe our efforts to target the chromodomain of M-phase phosphoprotein 8 (MPP8), a member of the human silencing hub (HUSH) complex and a histone 3 lysine 9 trimethyl (H3K9me3) reader that is vital for heterochromatin formation and has specific roles in cancer metastasis. Utilizing a one-bead, one-compound (OBOC) combinatorial screening approach, we identified UNC5246, a peptidomimetic ligand capable of interacting with the MPP8 chromodomain in the context of the HUSH complex. Additionally, a biotinylated derivative of UNC5246 facilitated chemoproteomics studies which revealed hepatoma-derived growth factor-related protein 2 (HRP2) as a novel protein associated with MPP8. HRP2 was further shown to colocalize with MPP8 at the E-cadherin gene locus, suggesting a possible role in cancer cell plasticity.
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A Peptidomimetic Ligand Targeting the Chromodomain of MPP8 Reveals HRP2's Association with the HUSH Complex.,Waybright JM, Clinkscales SE, Barnash KD, Budziszewski GR, Rectenwald JM, Chiarella AM, Norris-Drouin JL, Cholensky SH, Pearce KH, Herring LE, McGinty RK, Hathaway NA, James LI ACS Chem Biol. 2021 Sep 17;16(9):1721-1736. doi: 10.1021/acschembio.1c00429. Epub , 2021 Aug 20. PMID:34415726<ref>PMID:34415726</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 7m5u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Budziszewski GR]]
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[[Category: James LI]]
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[[Category: McGinty RK]]
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[[Category: Norris JL]]
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[[Category: Waybright JM]]

Current revision

Crystal structure of human MPP8 chromodomain in complex with peptidomimetic ligand UNC5246

PDB ID 7m5u

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