2as5

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[[Image:2as5.gif|left|200px]]
 
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{{Structure
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==Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.==
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|PDB= 2as5 |SIZE=350|CAPTION= <scene name='initialview01'>2as5</scene>, resolution 2.7&Aring;
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<StructureSection load='2as5' size='340' side='right'caption='[[2as5]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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<table><tr><td colspan='2'>[[2as5]] is a 8 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=2AS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AS5 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE= NFATC2, NFAT1, NFATP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FOXP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2as5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2as5 OCA], [https://pdbe.org/2as5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2as5 RCSB], [https://www.ebi.ac.uk/pdbsum/2as5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2as5 ProSAT]</span></td></tr>
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</table>
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'''Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.'''
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== Function ==
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[https://www.uniprot.org/uniprot/NFAC2_HUMAN NFAC2_HUMAN] Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway.<ref>PMID:21871017</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/as/2as5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2as5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Antigen stimulation of immune cells activates the transcription factor NFAT, a key regulator of T cell activation and anergy. NFAT forms cooperative complexes with the AP-1 family of transcription factors and regulates T cell activation-associated genes. Here we show that regulatory T cell (Treg) function is mediated by an analogous cooperative complex of NFAT with the forkhead transcription factor FOXP3, a lineage specification factor for Tregs. The crystal structure of an NFAT:FOXP2:DNA complex reveals an extensive protein-protein interaction interface between NFAT and FOXP2. Structure-guided mutations of FOXP3, predicted to progressively disrupt its interaction with NFAT, interfere in a graded manner with the ability of FOXP3 to repress expression of the cytokine IL2, upregulate expression of the Treg markers CTLA4 and CD25, and confer suppressor function in a murine model of autoimmune diabetes. Thus by switching transcriptional partners, NFAT converts the acute T cell activation program into the suppressor program of Tregs.
Antigen stimulation of immune cells activates the transcription factor NFAT, a key regulator of T cell activation and anergy. NFAT forms cooperative complexes with the AP-1 family of transcription factors and regulates T cell activation-associated genes. Here we show that regulatory T cell (Treg) function is mediated by an analogous cooperative complex of NFAT with the forkhead transcription factor FOXP3, a lineage specification factor for Tregs. The crystal structure of an NFAT:FOXP2:DNA complex reveals an extensive protein-protein interaction interface between NFAT and FOXP2. Structure-guided mutations of FOXP3, predicted to progressively disrupt its interaction with NFAT, interfere in a graded manner with the ability of FOXP3 to repress expression of the cytokine IL2, upregulate expression of the Treg markers CTLA4 and CD25, and confer suppressor function in a murine model of autoimmune diabetes. Thus by switching transcriptional partners, NFAT converts the acute T cell activation program into the suppressor program of Tregs.
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==Disease==
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FOXP3 controls regulatory T cell function through cooperation with NFAT.,Wu Y, Borde M, Heissmeyer V, Feuerer M, Lapan AD, Stroud JC, Bates DL, Guo L, Han A, Ziegler SF, Mathis D, Benoist C, Chen L, Rao A Cell. 2006 Jul 28;126(2):375-87. PMID:16873067<ref>PMID:16873067</ref>
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Known diseases associated with this structure: Speech-language disorder-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605317 605317]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2AS5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AS5 OCA].
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</div>
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<div class="pdbe-citations 2as5" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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FOXP3 controls regulatory T cell function through cooperation with NFAT., Wu Y, Borde M, Heissmeyer V, Feuerer M, Lapan AD, Stroud JC, Bates DL, Guo L, Han A, Ziegler SF, Mathis D, Benoist C, Chen L, Rao A, Cell. 2006 Jul 28;126(2):375-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16873067 16873067]
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*[[FOX 3D structures|FOX 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bates, D L.]]
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[[Category: Bates DL]]
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[[Category: Borde, M.]]
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[[Category: Borde M]]
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[[Category: Chen, L.]]
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[[Category: Chen L]]
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[[Category: Guo, L.]]
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[[Category: Guo L]]
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[[Category: Han, A.]]
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[[Category: Han A]]
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[[Category: Rao, A.]]
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[[Category: Rao A]]
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[[Category: Stroud, J C.]]
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[[Category: Stroud JC]]
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[[Category: Wu, Y.]]
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[[Category: Wu Y]]
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[[Category: MG]]
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[[Category: b-dna]]
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[[Category: forkhead domain]]
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[[Category: ig fold]]
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[[Category: rel homology region]]
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[[Category: rhr domain]]
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[[Category: winged helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:53:14 2008''
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Current revision

Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.

PDB ID 2as5

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