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| | <StructureSection load='3hfh' size='340' side='right'caption='[[3hfh]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3hfh' size='340' side='right'caption='[[3hfh]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hfh]] is a 2 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=3HFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hfh]] is a 2 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=3HFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFH FirstGlance]. <br> |
| - | </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>, <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]] 2.703Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA150, TAF2S, TCERG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <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=3hfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfh OCA], [https://pdbe.org/3hfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfh RCSB], [https://www.ebi.ac.uk/pdbsum/3hfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfh 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=3hfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfh OCA], [https://pdbe.org/3hfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfh RCSB], [https://www.ebi.ac.uk/pdbsum/3hfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TCRG1_HUMAN TCRG1_HUMAN]] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.<ref>PMID:9315662</ref> <ref>PMID:11604498</ref>
| + | [https://www.uniprot.org/uniprot/TCRG1_HUMAN TCRG1_HUMAN] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.<ref>PMID:9315662</ref> <ref>PMID:11604498</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bedford, M T]] | + | [[Category: Bedford MT]] |
| - | [[Category: Chen, X]] | + | [[Category: Chen X]] |
| - | [[Category: Jacobson, R H]] | + | [[Category: Jacobson RH]] |
| - | [[Category: Lu, M]] | + | [[Category: Lu M]] |
| - | [[Category: McMurray, J S]] | + | [[Category: McMurray JS]] |
| - | [[Category: Ren, Z]] | + | [[Category: Ren Z]] |
| - | [[Category: Subir, S]] | + | [[Category: Subir S]] |
| - | [[Category: Yang, J]] | + | [[Category: Yang J]] |
| - | [[Category: Activator]]
| + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Helix bundle]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Transcription regulator]]
| + | |
| Structural highlights
Function
TCRG1_HUMAN Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.[1] [2]
Publication Abstract from PubMed
FF domains are small protein-protein interaction modules that have two flanking conserved phenylalanine residues. They are present in proteins involved in transcription, RNA splicing, and signal transduction, and often exist in tandem arrays. Although several individual FF domain structures have been determined by NMR, the tandem nature of most FF domains has not been revealed. Here we report the 2.7-A-resolution crystal structure of the first three FF domains of the human transcription elongation factor CA150. Each FF domain is composed of three alpha-helices and a 3(10) helix between alpha-helix 2 and alpha-helix 3. The most striking feature of the structure is that an FF domain is connected to the next by an alpha-helix that continues from helix 3 to helix 1 of the next. The consequent elongated arrangement allows exposure of many charged residues within the region that can be engaged in interaction with other molecules. Binding studies using a peptide ligand suggest that a specific conformation of the FF domains might be required to achieve higher-affinity binding. Additionally, we explore potential DNA binding of the FF construct used in this study. Overall, we provide the first crystal structure of an FF domain and insights into the tandem nature of the FF domains and suggest that, in addition to protein binding, FF domains might be involved in DNA binding.
Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150.,Lu M, Yang J, Ren Z, Sabui S, Espejo A, Bedford MT, Jacobson RH, Jeruzalmi D, McMurray JS, Chen X J Mol Biol. 2009 Oct 23;393(2):397-408. Epub 2009 Aug 4. PMID:19660470[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sune C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA. CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription. Mol Cell Biol. 1997 Oct;17(10):6029-39. PMID:9315662
- ↑ Goldstrohm AC, Albrecht TR, Sune C, Bedford MT, Garcia-Blanco MA. The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Mol Cell Biol. 2001 Nov;21(22):7617-28. PMID:11604498 doi:10.1128/MCB.21.22.7617-7628.2001
- ↑ Lu M, Yang J, Ren Z, Sabui S, Espejo A, Bedford MT, Jacobson RH, Jeruzalmi D, McMurray JS, Chen X. Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150. J Mol Biol. 2009 Oct 23;393(2):397-408. Epub 2009 Aug 4. PMID:19660470 doi:10.1016/j.jmb.2009.07.086
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