1pd7

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{{Seed}}
 
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[[Image:1pd7.png|left|200px]]
 
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==Extended SID of Mad1 bound to the PAH2 domain of mSin3B==
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The line below this paragraph, containing "STRUCTURE_1pd7", creates the "Structure Box" on the page.
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<StructureSection load='1pd7' size='340' side='right'caption='[[1pd7]]' 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'>[[1pd7]] 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=1PD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PD7 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">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=1pd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pd7 OCA], [https://pdbe.org/1pd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pd7 RCSB], [https://www.ebi.ac.uk/pdbsum/1pd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pd7 ProSAT]</span></td></tr>
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{{STRUCTURE_1pd7| PDB=1pd7 | SCENE= }}
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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/pd/1pd7_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=1pd7 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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Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family. Here, we elaborate on the Mad-Sin3 interaction based on a binding study, solution structure, and dynamics of the PAH2 domain of mSin3 in complex to an extended Sin3 interacting domain (SID) of 24 residues of Mad1. We show that SID residues Met7 and Glu23, outside the previously defined minimal binding motif, mediate additional hydrophobic and electrostatic interactions with PAH2. On the basis of these results we propose an extended consensus sequence describing the PAH2-SID interaction specifically for the Mad family, showing that residues outside the hydrophobic core of the SID interact with PAH2 and modulate binding affinity to appropriate levels.
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===Extended SID of Mad1 bound to the PAH2 domain of mSin3B===
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Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins.,van Ingen H, Lasonder E, Jansen JF, Kaan AM, Spronk CA, Stunnenberg HG, Vuister GW Biochemistry. 2004 Jan 13;43(1):46-54. PMID:14705930<ref>PMID:14705930</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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The line below this paragraph, {{ABSTRACT_PUBMED_14705930}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1pd7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14705930 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14705930}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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1PD7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PD7 OCA].
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[[Category: Large Structures]]
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==Reference==
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Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins., van Ingen H, Lasonder E, Jansen JF, Kaan AM, Spronk CA, Stunnenberg HG, Vuister GW, Biochemistry. 2004 Jan 13;43(1):46-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14705930 14705930]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Jansen JF]]
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[[Category: Ingen, H Van.]]
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[[Category: Kaan AM]]
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[[Category: Jansen, J F.]]
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[[Category: Lasonder E]]
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[[Category: Kaan, A M.]]
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[[Category: Spronk CA]]
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[[Category: Lasonder, E.]]
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[[Category: Stunnenberg HG]]
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[[Category: Spronk, C A.]]
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[[Category: Van Ingen H]]
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[[Category: Stunnenberg, H G.]]
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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: Pah2]]
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[[Category: Protein-protein interaction]]
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[[Category: Sin3]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:24:19 2008''
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Current revision

Extended SID of Mad1 bound to the PAH2 domain of mSin3B

PDB ID 1pd7

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