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2n1u

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==Structure of SAP30L corepressor protein==
==Structure of SAP30L corepressor protein==
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<StructureSection load='2n1u' size='340' side='right' caption='[[2n1u]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
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<StructureSection load='2n1u' size='340' side='right'caption='[[2n1u]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2n1u]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2n1u]] is a 1 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=2N1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1U FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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">Solution NMR</td></tr>
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<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=2n1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1u OCA], [http://pdbe.org/2n1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1u RCSB], [http://www.ebi.ac.uk/pdbsum/2n1u PDBsum]</span></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=2n1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1u OCA], [https://pdbe.org/2n1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1u RCSB], [https://www.ebi.ac.uk/pdbsum/2n1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SP30L_HUMAN SP30L_HUMAN]] Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus.<ref>PMID:16820529</ref>
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[https://www.uniprot.org/uniprot/SP30L_HUMAN SP30L_HUMAN] Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus.<ref>PMID:16820529</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sin3A-associated protein 30-like (SAP30L) is one of the key proteins in a multi-subunit protein complex involved in transcriptional regulation via histone deacetylation. SAP30L, together with a highly homologous SAP30 as well as other SAP proteins (i.e., SAP25, SAP45, SAP130 and SAP180), is an essential component of the Sin3A corepressor complex, although its actual role has remained elusive. SAP30L is thought to function as an important stabilizing and bridging molecule in the complex and to mediate its interactions with other corepressors. SAP30L has been previously shown to contain an N-terminal Cys3 His type zinc finger (ZnF) motif, which is responsible for the key protein-protein, protein-DNA and protein-lipid interactions. By using high-resolution mass spectrometry, we studied a redox-dependent disulfide bond formation in SAP30L ZnF as a regulatory mechanism for its structure and function. We showed that upon oxidative stress SAP30L undergoes the formation of two specific disulfide bonds, a vicinal Cys29-Cys30 and Cys38-Cys74, with a concomitant release of the coordinated zinc ion. The oxidized protein was shown to remain folded in solution and to bind signaling phospholipids. We also determined a solution NMR structure for SAP30L ZnF that showed an overall fold similar to that of SAP30, determined earlier. The NMR titration experiments with lipids and DNA showed that the binding is mediated by the C-terminal tail as well as both alpha-helices of SAP30L ZnF. The implications of these results for the structure and function of SAP30L are discussed. This article is protected by copyright. All rights reserved.
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Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function.,Laitaoja M, Tossavainen H, Pihlajamaa T, Valjakka J, Viiri K, Lohi O, Permi P, Janis J Protein Sci. 2015 Nov 26. doi: 10.1002/pro.2849. PMID:26609676<ref>PMID:26609676</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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<div class="pdbe-citations 2n1u" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Permi, P]]
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[[Category: Homo sapiens]]
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[[Category: Tossavainen, H]]
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[[Category: Large Structures]]
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[[Category: Protein binding]]
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[[Category: Permi P]]
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[[Category: Tossavainen H]]

Current revision

Structure of SAP30L corepressor protein

PDB ID 2n1u

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