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| - | ==CRYSTAL STRUCTURE OF THE HUMAN TAF4-TAF12 (TAFII135-TAFII20) COMPLEX== | + | |
| - | <StructureSection load='1h3o' size='340' side='right' caption='[[1h3o]], [[Resolution|resolution]] 2.30Å' scene=''> | + | ==Crystal Structure of the Human TAF4-TAF12 (TAFII135-TAFII20) Complex== |
| | + | <StructureSection load='1h3o' size='340' side='right'caption='[[1h3o]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h3o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H3O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h3o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3O FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=1h3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3o OCA], [http://pdbe.org/1h3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h3o RCSB], [http://www.ebi.ac.uk/pdbsum/1h3o PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1h3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3o OCA], [https://pdbe.org/1h3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3o RCSB], [https://www.ebi.ac.uk/pdbsum/1h3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TAF12_HUMAN TAF12_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. | + | [https://www.uniprot.org/uniprot/TAF4_HUMAN TAF4_HUMAN] Makes part of TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/1h3o_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/1h3o_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Mitschler, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Moras, D]] | + | [[Category: Mitschler A]] |
| - | [[Category: Werten, S]] | + | [[Category: Moras D]] |
| - | [[Category: Histone fold domain]] | + | [[Category: Werten S]] |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Rna polymerase ii transcription]]
| + | |
| - | [[Category: Tbp-associated factor]]
| + | |
| - | [[Category: Tfiid]]
| + | |
| - | [[Category: Transcription-tbp-associated factors complex]]
| + | |
| - | [[Category: Transcription/tbp-associated factor]]
| + | |
| Structural highlights
Function
TAF4_HUMAN Makes part of TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone.
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
The crystal structure is presented of a complex formed by the interacting domains from two subunits of the general transcription factor TFIID, the human TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20). In agreement with predictions, hTAF12 forms a histone fold that is very similar to that of histone H2B, yet unexpected differences are observed between the structures of the hTAF12 interaction domain of hTAF4 and histone H2A. Most importantly, the hTAF4 fragment forms only the first two helices of a classical histone fold, which are followed by a 26-residue disordered region. This indicates that either full-length TAF4 contains an unusually long connecting loop between its second and third helix, and this helix is not required for stable interaction with TAF12, or that TAF4 represents a novel class of partial histone fold motifs. Structural models and structure-based sequence alignments support a role for TAF4b and hSTAF42/yADA1 as alternative partners for TAF12 and are consistent with the formation of nucleosome-like histone-fold octamers through interaction of TAF12 with a TAF6-TAF9 tetramer, yet argue against involvement of TAF12-containing histone-fold pairs in DNA binding.
Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20).,Werten S, Mitschler A, Romier C, Gangloff YG, Thuault S, Davidson I, Moras D J Biol Chem. 2002 Nov 22;277(47):45502-9. Epub 2002 Sep 16. PMID:12237304[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Werten S, Mitschler A, Romier C, Gangloff YG, Thuault S, Davidson I, Moras D. Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20). J Biol Chem. 2002 Nov 22;277(47):45502-9. Epub 2002 Sep 16. PMID:12237304 doi:http://dx.doi.org/10.1074/jbc.M206587200
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