2odd

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{{STRUCTURE_2odd| PDB=2odd | SCENE= }}
 
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===Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor===
 
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{{ABSTRACT_PUBMED_17560331}}
 
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==Disease==
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==Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor==
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[[http://www.uniprot.org/uniprot/MTG8_HUMAN MTG8_HUMAN]] Note=A chromosomal aberration involving RUNX1T1 is a cause of acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1/AML1.<ref>PMID:8334990</ref><ref>PMID:7541640</ref><ref>PMID:8353289</ref><ref>PMID:1423235</ref> Defects in RUNX1T1 may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].
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<StructureSection load='2odd' size='340' side='right'caption='[[2odd]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2odd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODD 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">Solution NMR</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=ZN:ZINC+ION'>ZN</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=2odd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odd OCA], [https://pdbe.org/2odd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odd RCSB], [https://www.ebi.ac.uk/pdbsum/2odd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NCOR2_HUMAN NCOR2_HUMAN] Transcriptional corepressor of NR4A2/NURR1 and acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state (By similarity). Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors.
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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/od/2odd_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=2odd 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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AML1/ETO results from the t(8;21) associated with 12%-15% of acute myeloid leukemia. The AML1/ETO MYND domain mediates interactions with the corepressors SMRT and N-CoR and contributes to AML1/ETO's ability to repress proliferation and differentiation of primary bone marrow cells as well as to enhance their self renewal in vitro. We solved the solution structure of the MYND domain and show it to be structurally homologous to the PHD and RING finger families of proteins. We also determined the solution structure of an MYND-SMRT peptide complex. We demonstrated that a single amino acid substitution that disrupts the interaction between the MYND domain and the SMRT peptide attenuated AML1/ETO's effects on proliferation, differentiation, and gene expression.
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==Function==
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Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity.,Liu Y, Chen W, Gaudet J, Cheney MD, Roudaia L, Cierpicki T, Klet RC, Hartman K, Laue TM, Speck NA, Bushweller JH Cancer Cell. 2007 Jun;11(6):483-97. PMID:17560331<ref>PMID:17560331</ref>
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[[http://www.uniprot.org/uniprot/MTG8_HUMAN MTG8_HUMAN]] Transcription regulator that excerts its function by binding to histone deacetylases and transcription factors. Can repress transactivation mediated by TCF12.<ref>PMID:10973986</ref><ref>PMID:16803958</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2odd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODD OCA].
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</div>
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<div class="pdbe-citations 2odd" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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<ref group="xtra">PMID:017560331</ref><references group="xtra"/><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: Bushweller, J H.]]
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[[Category: Large Structures]]
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[[Category: Chen, W.]]
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[[Category: Bushweller JH]]
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[[Category: Cheney, M D.]]
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[[Category: Chen W]]
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[[Category: Cierpicki, T.]]
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[[Category: Cheney MD]]
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[[Category: Gaudet, J.]]
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[[Category: Cierpicki T]]
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[[Category: Hartman, K.]]
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[[Category: Gaudet J]]
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[[Category: Klet, R C.]]
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[[Category: Hartman K]]
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[[Category: Laue, T M.]]
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[[Category: Klet RC]]
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[[Category: Liu, Y Z.]]
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[[Category: Laue TM]]
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[[Category: Roudaia, L.]]
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[[Category: Liu YZ]]
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[[Category: Speck, N A.]]
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[[Category: Roudaia L]]
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[[Category: Cross-braced topology]]
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[[Category: Speck NA]]
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[[Category: Metal binding protein]]
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[[Category: Mynd zinc finger]]
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[[Category: Poly-proline]]
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[[Category: Proline-tryptophan interaction]]
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Current revision

Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor

PDB ID 2odd

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