2ld7: Difference between revisions
New page: '''Unreleased structure''' The entry 2ld7 is ON HOLD Authors: Xie, T., He, Y., Korkeamaki, H., Zhang, Y., Imhoff, R., Lohi, O., Radhakrishnan, I. Description: solution structure of the... |
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The | ==Solution structure of the mSin3A PAH3-SAP30 SID complex== | ||
<StructureSection load='2ld7' size='340' side='right'caption='[[2ld7]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ld7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ld7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld7 OCA], [https://pdbe.org/2ld7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAP30_MOUSE SAP30_MOUSE] Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones.<ref>PMID:9702189</ref> [UniProtKB:O75446] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The approximately 2-megadalton evolutionarily conserved histone deacetylase-associated Rpd3L/Sin3L complex plays critical roles in altering the histone code and repressing transcription of a broad range of genes involved in many aspects of cellular physiology. Targeting of this complex to specific regions of the genome is presumed to rely on interactions involving one or more of at least 10 distinct subunits in the complex. Here we describe the solution structure of the complex formed by the interacting domains of two constitutively associated subunits, mSin3A and SAP30. The mSin3A paired amphipathic helix 3 (PAH3) domain in the complex adopts the left-handed four-helix bundle structure characteristic of PAH domains. The SAP30 Sin3 interaction domain (SID) binds to PAH3 via a tripartite structural motif, including a C-terminal helix that targets the canonical PAH hydrophobic cleft while two other helices and an N-terminal extension target a discrete surface formed largely by the PAH3 alpha2, alpha3, and alpha3' helices. The protein-protein interface is extensive ( approximately 1400 A(2)), accounting for the high affinity of the interaction and the constitutive association of the SAP30 subunit with the Rpd3L/Sin3L complex. We further show using NMR that the mSin3A PAH3-SAP30 SID complex can bind to nucleic acids, hinting at a role for a nucleolar localization sequence in the SID alphaA helix in targeting the Rpd3L/Sin3L complex for silencing ribosomal RNA genes. | |||
Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding.,Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I J Biol Chem. 2011 Aug 5;286(31):27814-24. Epub 2011 Jun 15. PMID:21676866<ref>PMID:21676866</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ld7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: He Y]] | |||
[[Category: Imhoff R]] | |||
[[Category: Korkeamaki H]] | |||
[[Category: Lohi O]] | |||
[[Category: Radhakrishnan I]] | |||
[[Category: Xie T]] | |||
[[Category: Zhang Y]] | |||
Latest revision as of 08:41, 15 May 2024
Solution structure of the mSin3A PAH3-SAP30 SID complexSolution structure of the mSin3A PAH3-SAP30 SID complex
Structural highlights
FunctionSAP30_MOUSE Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones.[1] [UniProtKB:O75446] Publication Abstract from PubMedThe approximately 2-megadalton evolutionarily conserved histone deacetylase-associated Rpd3L/Sin3L complex plays critical roles in altering the histone code and repressing transcription of a broad range of genes involved in many aspects of cellular physiology. Targeting of this complex to specific regions of the genome is presumed to rely on interactions involving one or more of at least 10 distinct subunits in the complex. Here we describe the solution structure of the complex formed by the interacting domains of two constitutively associated subunits, mSin3A and SAP30. The mSin3A paired amphipathic helix 3 (PAH3) domain in the complex adopts the left-handed four-helix bundle structure characteristic of PAH domains. The SAP30 Sin3 interaction domain (SID) binds to PAH3 via a tripartite structural motif, including a C-terminal helix that targets the canonical PAH hydrophobic cleft while two other helices and an N-terminal extension target a discrete surface formed largely by the PAH3 alpha2, alpha3, and alpha3' helices. The protein-protein interface is extensive ( approximately 1400 A(2)), accounting for the high affinity of the interaction and the constitutive association of the SAP30 subunit with the Rpd3L/Sin3L complex. We further show using NMR that the mSin3A PAH3-SAP30 SID complex can bind to nucleic acids, hinting at a role for a nucleolar localization sequence in the SID alphaA helix in targeting the Rpd3L/Sin3L complex for silencing ribosomal RNA genes. Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding.,Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I J Biol Chem. 2011 Aug 5;286(31):27814-24. Epub 2011 Jun 15. PMID:21676866[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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