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2hde

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Revision as of 06:51, 27 June 2018

Solution Structure of Human SAP18

Structural highlights

2hde 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.
Gene:	SAP18 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SAP18_HUMAN] Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism.^[1]

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

Signal transduction pathways are frequently found to repress transcription of target genes in the absence of stimulation and, conversely, to upregulate transcription in the presence of a signal. Transcription factors are central in this dual regulatory mechanism and widely use a generalized mechanism to repress transcription through recruitment of a Sin3-histone deacetylase (HDAC) complex to their binding sites on DNA. The protein SAP18 (Sin3-associated polypeptide of 18 kDa) has been shown to play a key role in gene-specific recruitment of the HDAC complex by a number of transcription factors including Gli, GAGA, and Bicoid. The solution structure of SAP18 reveals a ubiquitin-like fold with several large loop insertions relative to other family members. This fold supports the functional role of SAP18 as a protein-protein adapter module and provides insight for how SAP18 may bridge the Sin3-HDAC complex to transcription factors.

Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly.,McCallum SA, Bazan JF, Merchant M, Yin J, Pan B, de Sauvage FJ, Fairbrother WJ Biochemistry. 2006 Oct 3;45(39):11974-82. PMID:17002296^[2]

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

References

↑ Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell. 1997 May 2;89(3):357-64. PMID:9150135
↑ McCallum SA, Bazan JF, Merchant M, Yin J, Pan B, de Sauvage FJ, Fairbrother WJ. Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly. Biochemistry. 2006 Oct 3;45(39):11974-82. PMID:17002296 doi:http://dx.doi.org/10.1021/bi060687l

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hde"

@@ Line 1: / Line 1: @@
 ==Solution Structure of Human SAP18==
 <StructureSection load='2hde' size='340' side='right' caption='[[2hde]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2hde]] 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=2HDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HDE FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAP18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hde OCA], [http://pdbe.org/2hde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hde RCSB], [http://www.ebi.ac.uk/pdbsum/2hde PDBsum]</span></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=2hde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hde OCA], [http://pdbe.org/2hde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hde RCSB], [http://www.ebi.ac.uk/pdbsum/2hde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hde ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/2hde_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/2hde_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=2hde ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2hde

From Proteopedia

Revision as of 06:51, 27 June 2018

Solution Structure of Human SAP18

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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