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| | ==Crystal structure of the Ets1 dimer DNA complex.== | | ==Crystal structure of the Ets1 dimer DNA complex.== |
| - | <StructureSection load='2nny' size='340' side='right' caption='[[2nny]], [[Resolution|resolution]] 2.58Å' scene=''> | + | <StructureSection load='2nny' size='340' side='right'caption='[[2nny]], [[Resolution|resolution]] 2.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nny]] 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=2NNY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NNY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nny]] is a 4 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=2NNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k78|1k78]], [[1gvj|1gvj]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k78|1k78]], [[1gvj|1gvj]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETS1 ([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">ETS1 ([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=2nny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nny OCA], [http://pdbe.org/2nny PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nny RCSB], [http://www.ebi.ac.uk/pdbsum/2nny PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nny 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=2nny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nny OCA], [https://pdbe.org/2nny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nny RCSB], [https://www.ebi.ac.uk/pdbsum/2nny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nny ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ETS1_HUMAN ETS1_HUMAN]] Transcription factor.<ref>PMID:10698492</ref> | + | [[https://www.uniprot.org/uniprot/ETS1_HUMAN ETS1_HUMAN]] Transcription factor.<ref>PMID:10698492</ref> |
| | == 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: Kachalova, G S]] | | [[Category: Kachalova, G S]] |
| | [[Category: Lamber, E P]] | | [[Category: Lamber, E P]] |
| Structural highlights
Function
[ETS1_HUMAN] Transcription factor.[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
The function of the Ets-1 transcription factor is regulated by two regions that flank its DNA-binding domain. A previously established mechanism for auto-inhibition of monomeric Ets-1 on DNA response elements with a single ETS-binding site, however, has not been observed for the stromelysin-1 promoter containing two palindromic ETS-binding sites. We present the structure of Ets-1 on this promoter element, revealing a ternary complex in which protein homo-dimerization is mediated by the specific arrangement of the two ETS-binding sites. In this complex, the N-terminal-flanking region is required for ternary protein-DNA assembly. Ets-1 variants, in which residues from this region are mutated, loose the ability for DNA-mediated dimerization and stromelysin-1 promoter transactivation. Thus, our data unravel the molecular basis for relief of auto-inhibition and the ability of Ets-1 to function as a facultative dimeric transcription factor on this site. Our findings may also explain previous data of Ets-1 function in the context of heterologous transcription factors, thus providing a molecular model that could also be valid for Ets-1 regulation by hetero-oligomeric assembly.
Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization.,Lamber EP, Vanhille L, Textor LC, Kachalova GS, Sieweke MH, Wilmanns M EMBO J. 2008 Jul 23;27(14):2006-17. Epub 2008 Jun 19. PMID:18566588[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li R, Pei H, Watson DK, Papas TS. EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene. 2000 Feb 10;19(6):745-53. PMID:10698492 doi:10.1038/sj.onc.1203385
- ↑ Lamber EP, Vanhille L, Textor LC, Kachalova GS, Sieweke MH, Wilmanns M. Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization. EMBO J. 2008 Jul 23;27(14):2006-17. Epub 2008 Jun 19. PMID:18566588 doi:10.1038/emboj.2008.117
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