4zqa

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==Crystal Structure of the Sds3 Dimerization Domain==
==Crystal Structure of the Sds3 Dimerization Domain==
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<StructureSection load='4zqa' size='340' side='right' caption='[[4zqa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4zqa' size='340' side='right'caption='[[4zqa]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4zqa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZQA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4zqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZQA FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zqa RCSB], [http://www.ebi.ac.uk/pdbsum/4zqa PDBsum]</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]] 1.65&#8491;</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=4zqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zqa OCA], [https://pdbe.org/4zqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zqa RCSB], [https://www.ebi.ac.uk/pdbsum/4zqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zqa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SDS3_MOUSE SDS3_MOUSE]] Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity).
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[https://www.uniprot.org/uniprot/SDS3_MOUSE SDS3_MOUSE] Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acetylation is correlated with chromatin decondensation and transcriptional activation, but its regulation by histone deacetylase (HDAC)-bearing corepressor complexes is poorly understood. Here, we describe the mechanism of assembly of the mammalian Sin3L/Rpd3L complex facilitated by Sds3, a conserved subunit deemed critical for proper assembly. Sds3 engages a globular, helical region of the HDAC interaction domain (HID) of the scaffolding protein Sin3A through a bipartite motif comprising a helix and an adjacent extended segment. Sds3 dimerizes through not only one of the predicted coiled-coil motifs but also, the segment preceding it, forming an approximately 150-A-long antiparallel dimer. Contrary to previous findings in yeast, Sin3A rather than Sds3 functions in recruiting HDAC1 into the complex by engaging the latter through a highly conserved segment adjacent to the helical HID subdomain. In the resulting model for the ternary complex, the two copies of the HDACs are situated distally and dynamically because of a natively unstructured linker connecting the dimerization domain and the Sin3A interaction domain of Sds3; these features contrast with the static organization described previously for the NuRD (nucleosome remodeling and deacetylase) complex. The Sds3 linker features several conserved basic residues that could potentially maintain the complex on chromatin by nonspecific interactions with DNA after initial recruitment by sequence-specific DNA-binding repressors.
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Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex.,Clark MD, Marcum R, Graveline R, Chan CW, Xie T, Chen Z, Ding Y, Zhang Y, Mondragon A, David G, Radhakrishnan I Proc Natl Acad Sci U S A. 2015 Jun 29. pii: 201504021. PMID:26124119<ref>PMID:26124119</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chan, C W]]
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[[Category: Large Structures]]
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[[Category: Clark, M]]
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[[Category: Mus musculus]]
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[[Category: Mondragon, A]]
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[[Category: Chan CW]]
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[[Category: Radhakrishnan, I]]
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[[Category: Clark M]]
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[[Category: Coiled-coil]]
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[[Category: Mondragon A]]
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[[Category: Corepressor complex]]
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[[Category: Radhakrishnan I]]
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[[Category: Histone deacetylase complex]]
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[[Category: Transcription repression]]
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[[Category: Transcription repressor]]
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Current revision

Crystal Structure of the Sds3 Dimerization Domain

PDB ID 4zqa

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