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| ==haddock model of GATA1NF:Lmo2LIM2-Ldb1LID== | | ==haddock model of GATA1NF:Lmo2LIM2-Ldb1LID== |
- | <StructureSection load='2l6y' size='340' side='right'caption='[[2l6y]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2l6y' size='340' side='right'caption='[[2l6y]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2l6y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l6y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6Y FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l6z|2l6z]], [[2l3k|2l3k]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2l6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6y OCA], [https://pdbe.org/2l6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6y RCSB], [https://www.ebi.ac.uk/pdbsum/2l6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6y 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=2l6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6y OCA], [https://pdbe.org/2l6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6y RCSB], [https://www.ebi.ac.uk/pdbsum/2l6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6y ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/GATA1_MOUSE GATA1_MOUSE]] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.<ref>PMID:2276623</ref> <ref>PMID:8206977</ref> <ref>PMID:8524811</ref> <ref>PMID:15173587</ref> <ref>PMID:16888089</ref>
| + | [https://www.uniprot.org/uniprot/GATA1_MOUSE GATA1_MOUSE] Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.<ref>PMID:2276623</ref> <ref>PMID:8206977</ref> <ref>PMID:8524811</ref> <ref>PMID:15173587</ref> <ref>PMID:16888089</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
- | [[Category: Crossley, M]] | + | [[Category: Crossley M]] |
- | [[Category: Dastmalchi, S]] | + | [[Category: Dastmalchi S]] |
- | [[Category: Gamsjaeger, R]] | + | [[Category: Gamsjaeger R]] |
- | [[Category: Mackay, J P]] | + | [[Category: Mackay JP]] |
- | [[Category: Matthews, J M]] | + | [[Category: Matthews JM]] |
- | [[Category: Stokes, P H]] | + | [[Category: Stokes PH]] |
- | [[Category: Wienert, B]] | + | [[Category: Wienert B]] |
- | [[Category: Wilkinson-White, L]] | + | [[Category: Wilkinson-White L]] |
- | [[Category: Fog-1]]
| + | |
- | [[Category: Gata-1]]
| + | |
- | [[Category: Ldb1]]
| + | |
- | [[Category: Lmo2]]
| + | |
- | [[Category: Transcription regulation-oncoprotein complex]]
| + | |
| Structural highlights
Function
GATA1_MOUSE Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
The control of red blood cell and megakaryocyte development by the regulatory protein GATA1 is a paradigm for transcriptional regulation of gene expression in cell lineage differentiation and maturation. Most GATA1-regulated events require GATA1 to bind FOG1, and essentially all GATA1-activated genes are cooccupied by a TAL1/E2A/LMO2/LDB1 complex; however, it is not known whether FOG1 and TAL1/E2A/LMO2/LDB1 are simultaneously recruited by GATA1. Our structural data reveal that the FOG1-binding domain of GATA1, the N finger, can also directly contact LMO2 and show that, despite the small size (< 50 residues) of the GATA1 N finger, both FOG1 and LMO2 can simultaneously bind this domain. LMO2 in turn can simultaneously contact both GATA1 and the DNA-binding protein TAL1/E2A at bipartite E-box/WGATAR sites. Taken together, our data provide the first structural snapshot of multiprotein complex formation at GATA1-dependent genes and support a model in which FOG1 and TAL1/E2A/LMO2/LDB1 can cooccupy E-box/WGATAR sites to facilitate GATA1-mediated activation of gene activation.
Structural basis of simultaneous recruitment of the transcriptional regulators LMO2 and FOG1/ZFPM1 by the transcription factor GATA1.,Wilkinson-White L, Gamsjaeger R, Dastmalchi S, Wienert B, Stokes PH, Crossley M, Mackay JP, Matthews JM Proc Natl Acad Sci U S A. 2011 Aug 15. PMID:21844373[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martin DI, Orkin SH. Transcriptional activation and DNA binding by the erythroid factor GF-1/NF-E1/Eryf 1. Genes Dev. 1990 Nov;4(11):1886-98. PMID:2276623
- ↑ Crossley M, Orkin SH. Phosphorylation of the erythroid transcription factor GATA-1. J Biol Chem. 1994 Jun 17;269(24):16589-96. PMID:8206977
- ↑ Calligaris R, Bottardi S, Cogoi S, Apezteguia I, Santoro C. Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11598-602. PMID:8524811
- ↑ Collavin L, Gostissa M, Avolio F, Secco P, Ronchi A, Santoro C, Del Sal G. Modification of the erythroid transcription factor GATA-1 by SUMO-1. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8870-5. Epub 2004 Jun 1. PMID:15173587 doi:http://dx.doi.org/10.1073/pnas.0308605101
- ↑ Lamonica JM, Vakoc CR, Blobel GA. Acetylation of GATA-1 is required for chromatin occupancy. Blood. 2006 Dec 1;108(12):3736-8. Epub 2006 Aug 3. PMID:16888089 doi:http://dx.doi.org/10.1182/blood-2006-07-032847
- ↑ Wilkinson-White L, Gamsjaeger R, Dastmalchi S, Wienert B, Stokes PH, Crossley M, Mackay JP, Matthews JM. Structural basis of simultaneous recruitment of the transcriptional regulators LMO2 and FOG1/ZFPM1 by the transcription factor GATA1. Proc Natl Acad Sci U S A. 2011 Aug 15. PMID:21844373 doi:10.1073/pnas.1105898108
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