1pd7
From Proteopedia
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==Extended SID of Mad1 bound to the PAH2 domain of mSin3B== | ==Extended SID of Mad1 bound to the PAH2 domain of mSin3B== | ||
| - | <StructureSection load='1pd7' size='340' side='right'caption='[[1pd7 | + | <StructureSection load='1pd7' size='340' side='right'caption='[[1pd7]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pd7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pd7" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | + | [[Category: Jansen JF]] | |
| - | [[Category: Jansen | + | [[Category: Kaan AM]] |
| - | [[Category: Kaan | + | [[Category: Lasonder E]] |
| - | [[Category: Lasonder | + | [[Category: Spronk CA]] |
| - | [[Category: Spronk | + | [[Category: Stunnenberg HG]] |
| - | [[Category: Stunnenberg | + | [[Category: Van Ingen H]] |
| - | [[Category: | + | [[Category: Vuister GW]] |
| - | [[Category: | + | |
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Revision as of 05:54, 17 April 2024
Extended SID of Mad1 bound to the PAH2 domain of mSin3B
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