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1e91

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(New page: 200px<br /> <applet load="1e91" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e91" /> '''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B ...)
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[[Image:1e91.gif|left|200px]]<br />
 
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<applet load="1e91" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e91" />
 
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'''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br />
 
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==Overview==
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==Structure of the complex of the Mad1-Sin3B interaction domains==
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Sin3A or Sin3B are components of a corepressor complex that mediates, repression by transcription factors such as the helix-loop-helix proteins, Mad and Mxi. Members of the Mad/Mxi family of repressors play important, roles in the transition between proliferation and differentiation by, down-regulating the expression of genes that are activated by the, proto-oncogene product Myc. Here, we report the solution structure of the, second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex, with a peptide comprising the N-terminal region of Mad1. This complex, exhibits a novel interaction fold for which we propose the name 'wedged, helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that, accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized., The PAH2-Mad1 structure provides the basis for determining the principles, of protein interaction and selectivity involving PAH domains.
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<StructureSection load='1e91' size='340' side='right'caption='[[1e91]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e91]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E91 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e91 OCA], [https://pdbe.org/1e91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e91 RCSB], [https://www.ebi.ac.uk/pdbsum/1e91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e91 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SIN3B_MOUSE SIN3B_MOUSE] Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription.<ref>PMID:7889570</ref> <ref>PMID:10620510</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/e9/1e91_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=1e91 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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Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. The PAH2-Mad1 structure provides the basis for determining the principles of protein interaction and selectivity involving PAH domains.
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==Disease==
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The Mad1-Sin3B interaction involves a novel helical fold.,Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW Nat Struct Biol. 2000 Dec;7(12):1100-4. PMID:11101889<ref>PMID:11101889</ref>
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Known diseases associated with this structure: Lymphoma, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602686 602686]], Prostate cancer, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602686 602686]]
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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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1E91 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA].
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</div>
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<div class="pdbe-citations 1e91" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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The Mad1-Sin3B interaction involves a novel helical fold., Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW, Nat Struct Biol. 2000 Dec;7(12):1100-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11101889 11101889]
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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: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Jansen JFA]]
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[[Category: Jansen, J.F.A.]]
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[[Category: Kaan AM]]
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[[Category: Kaan, A.M.]]
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[[Category: Spronk CAEM]]
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[[Category: Spronk, C.A.E.M.]]
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[[Category: Stunnenberg HG]]
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[[Category: Stunnenberg, H.G.]]
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[[Category: Tessari M]]
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[[Category: Tessari, M.]]
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[[Category: Vermeulen M]]
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[[Category: Vermeulen, M.]]
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[[Category: Vuister GW]]
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[[Category: Vuister, G.W.]]
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[[Category: eukaryotic transcriptional regulation]]
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[[Category: mad1]]
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[[Category: pah domains]]
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[[Category: protein-protein interactions]]
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[[Category: sin3]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:41:03 2007''
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Current revision

Structure of the complex of the Mad1-Sin3B interaction domains

PDB ID 1e91

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