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| | <StructureSection load='2c62' size='340' side='right'caption='[[2c62]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='2c62' size='340' side='right'caption='[[2c62]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c62]] is a 3 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=2C62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C62 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c62]] is a 3 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=2C62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C62 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pcf|1pcf]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c62 OCA], [https://pdbe.org/2c62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c62 RCSB], [https://www.ebi.ac.uk/pdbsum/2c62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c62 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=2c62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c62 OCA], [https://pdbe.org/2c62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c62 RCSB], [https://www.ebi.ac.uk/pdbsum/2c62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c62 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TCP4_HUMAN TCP4_HUMAN] General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA).<ref>PMID:8062392</ref> <ref>PMID:8062391</ref> <ref>PMID:7628453</ref> <ref>PMID:9482861</ref> <ref>PMID:16689930</ref> <ref>PMID:9360603</ref> <ref>PMID:16605275</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Moras, D]] | + | [[Category: Moras D]] |
| - | [[Category: Werten, S]] | + | [[Category: Werten S]] |
| - | [[Category: Activator]]
| + | |
| - | [[Category: Dna unwinding]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| - | [[Category: Single-stranded dna]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription cofactor]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
TCP4_HUMAN General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. May be involved in stabilizing the multiprotein transcription complex. Binds single-stranded DNA. Also binds, in vitro, non-specifically to double-stranded DNA (ds DNA).[1] [2] [3] [4] [5] [6] [7]
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 1.74-A crystal structure of the human transcription cofactor PC4 in complex with a single-stranded 20-mer oligonucleotide reveals how symmetry-related beta-surfaces of the protein homodimer interact with juxtaposed 5-nucleotide DNA regions running in opposite directions. The structure explains high-affinity binding of PC4 to the complementary strands of unwinding duplex DNA, and it suggests the cofactor may have a role in relaxing negative supercoils or exposing unpaired bases for sequence-specific recognition by other biomolecules.
A global transcription cofactor bound to juxtaposed strands of unwound DNA.,Werten S, Moras D Nat Struct Mol Biol. 2006 Feb;13(2):181-2. Epub 2006 Jan 15. PMID:16415882[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kretzschmar M, Kaiser K, Lottspeich F, Meisterernst M. A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators. Cell. 1994 Aug 12;78(3):525-34. PMID:8062392
- ↑ Ge H, Roeder RG. Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes. Cell. 1994 Aug 12;78(3):513-23. PMID:8062391
- ↑ Kaiser K, Stelzer G, Meisterernst M. The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation. EMBO J. 1995 Jul 17;14(14):3520-7. PMID:7628453
- ↑ Malik S, Guermah M, Roeder RG. A dynamic model for PC4 coactivator function in RNA polymerase II transcription. Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2192-7. PMID:9482861
- ↑ Jonker HR, Wechselberger RW, Pinkse M, Kaptein R, Folkers GE. Gradual phosphorylation regulates PC4 coactivator function. FEBS J. 2006 Apr;273(7):1430-44. PMID:16689930 doi:http://dx.doi.org/10.1111/j.1742-4658.2006.05165.x
- ↑ Brandsen J, Werten S, van der Vliet PC, Meisterernst M, Kroon J, Gros P. C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site. Nat Struct Biol. 1997 Nov;4(11):900-3. PMID:9360603
- ↑ Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. Biochemistry. 2006 Apr 18;45(15):5067-81. PMID:16605275 doi:http://dx.doi.org/10.1021/bi052531b
- ↑ Werten S, Moras D. A global transcription cofactor bound to juxtaposed strands of unwound DNA. Nat Struct Mol Biol. 2006 Feb;13(2):181-2. Epub 2006 Jan 15. PMID:16415882 doi:10.1038/nsmb1044
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