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| | ==Structure of TAFH domain of the human TAF4 subunit of TFIID== | | ==Structure of TAFH domain of the human TAF4 subunit of TFIID== |
| - | <StructureSection load='2p6v' size='340' side='right' caption='[[2p6v]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2p6v' size='340' side='right'caption='[[2p6v]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2p6v]] is a 1 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=2P6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P6V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2p6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P6V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 ([https://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=2p6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6v OCA], [http://pdbe.org/2p6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p6v RCSB], [http://www.ebi.ac.uk/pdbsum/2p6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p6v ProSAT]</span></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=2p6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6v OCA], [https://pdbe.org/2p6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p6v RCSB], [https://www.ebi.ac.uk/pdbsum/2p6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p6v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [[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]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Jacobson, R H]] | | [[Category: Jacobson, R H]] |
| | [[Category: Matsumura, T]] | | [[Category: Matsumura, T]] |
| Structural highlights
2p6v is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| NonStd Res: | |
| Gene: | TAF4, TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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
TBP-associated factor 4 (TAF4), an essential subunit of the TFIID complex acts as a coactivator for multiple transcriptional regulators, including Sp1 and CREB. However, little is known regarding the structural properties of the TAF4 subunit that lead to the coactivator function. Here, we report the crystal structure at 2.0-A resolution of the human TAF4-TAFH domain, a conserved domain among all metazoan TAF4, TAF4b, and ETO family members. The hTAF4-TAFH structure adopts a completely helical fold with a large hydrophobic groove that forms a binding surface for TAF4 interacting factors. Using peptide phage display, we have characterized the binding preference of the hTAF4-TAFH domain for a hydrophobic motif, DPsiPsizetazetaPsiPhi, that is present in a number of nuclear factors, including several important transcriptional regulators with roles in activating, repressing, and modulating posttranslational modifications. A comparison of the hTAF4-TAFH structure with the homologous ETO-TAFH domain reveals several critical residues important for hTAF4-TAFH target specificity and suggests that TAF4 has evolved in response to the increased transcriptional complexity of metazoans.
Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.,Wang X, Truckses DM, Takada S, Matsumura T, Tanese N, Jacobson RH Proc Natl Acad Sci U S A. 2007 May 8;104(19):7839-44. Epub 2007 May 1. PMID:17483474[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Truckses DM, Takada S, Matsumura T, Tanese N, Jacobson RH. Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Proc Natl Acad Sci U S A. 2007 May 8;104(19):7839-44. Epub 2007 May 1. PMID:17483474
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