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1xc5

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Revision as of 21:21, 10 September 2015

Solution Structure of the SMRT Deacetylase Activation Domain

Structural highlights

1xc5 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[NCOR2_HUMAN] Transcriptional corepressor of NR4A2/NURR1 and acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state (By similarity). Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) and NCoR (nuclear receptor corepressor) are transcriptional corepressors that play an essential role in the regulation of development and metabolism. This role is achieved, in part, through the recruitment of a key histone deacetylase (HDAC3), which is itself indispensable for cell viability. The assembly of HDAC3 with the deacetylase activation domain (DAD) of SMRT and NCoR is required for activation of the otherwise inert deacetylase. The DAD comprises an N-terminal DAD-specific motif and a C-terminal SANT (SWI3/ADA2/NCoR/TFIIIB)-like domain. We report here the solution structure of the DAD from SMRT, which reveals a four-helical structure. The DAD differs from the SANT (and MYB) domains in that (i) it has an additional N-terminal helix and (ii) there is a notable hydrophobic groove on the surface of the domain. Structure-guided mutagenesis, combined with interaction assays, showed that residues in the vicinity of the hydrophobic groove are required for interaction with (and hence activation of) HDAC3. Importantly, one surface-exposed lysine is required for activation of HDAC3, but not for interaction. This lysine may play a uniquely important role in the mechanism of activating HDAC3.

Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors.,Codina A, Love JD, Li Y, Lazar MA, Neuhaus D, Schwabe JW Proc Natl Acad Sci U S A. 2005 Apr 26;102(17):6009-14. Epub 2005 Apr 18. PMID:15837933^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Codina A, Love JD, Li Y, Lazar MA, Neuhaus D, Schwabe JW. Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors. Proc Natl Acad Sci U S A. 2005 Apr 26;102(17):6009-14. Epub 2005 Apr 18. PMID:15837933

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xc5"

@@ Line 2: / Line 2: @@
 <StructureSection load='1xc5' size='340' side='right' caption='[[1xc5]], [[NMR_Ensembles_of_Models | 28 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XC5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XC5 FirstGlance]. <br>
-</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=1xc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xc5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1xc5 PDBsum]</span></td></tr>
+</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=1xc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xc5 OCA], [http://pdbe.org/1xc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1xc5 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1xc5" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Codina, A]]
 [[Category: Lazar, M A]]

1xc5

From Proteopedia

Revision as of 21:21, 10 September 2015

Solution Structure of the SMRT Deacetylase Activation Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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