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3qrf

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Structure of a domain-swapped FOXP3 dimer

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Retrieved from "http://52.214.119.220/wiki/index.php/3qrf"

@@ Line 3: / Line 3: @@
 <StructureSection load='3qrf' size='340' side='right'caption='[[3qrf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qrf]] is a 10 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=3QRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qrf]] is a 10 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=3QRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QRF FirstGlance]. <br>
-</td></tr><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a02|1a02]], [[1owr|1owr]], [[2as5|2as5]], [[2a07|2a07]]</div></td></tr>
+<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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFATC2, NFAT1, NFATP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FOXP3, IPEX, JM2 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrf OCA], [https://pdbe.org/3qrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qrf RCSB], [https://www.ebi.ac.uk/pdbsum/3qrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qrf ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[https://www.uniprot.org/uniprot/FOXP3_HUMAN FOXP3_HUMAN]] Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[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>  [[https://www.uniprot.org/uniprot/FOXP3_HUMAN FOXP3_HUMAN]] Probable transcription factor. Plays a critical role in the control of immune response.
+[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The transcription factor FOXP3 is essential for the suppressive function of regulatory T cells that are required for maintaining self-tolerance. We have solved the crystal structure of the FOXP3 forkhead domain as a ternary complex with the DNA-binding domain of the transcription factor NFAT1 and a DNA oligonucleotide from the interleukin-2 promoter. A striking feature of this structure is that FOXP3 forms a domain-swapped dimer that bridges two molecules of DNA. Structure-guided or autoimmune disease (IPEX)-associated mutations in the domain-swap interface diminished dimer formation by the FOXP3 forkhead domain without compromising FOXP3 DNA binding. These mutations also eliminated T cell-suppressive activity conferred by FOXP3, both in vitro and in a murine model of autoimmune diabetes in vivo. We conclude that FOXP3-mediated suppressor function requires dimerization through the forkhead domain and that mutations in the dimer interface can lead to the systemic autoimmunity observed in IPEX patients.
-Structure of a Domain-Swapped FOXP3 Dimer on DNA and Its Function in Regulatory T Cells.,Bandukwala HS, Wu Y, Feurer M, Chen Y, Barbosa B, Ghosh S, Stroud JC, Benoist C, Mathis D, Rao A, Chen L Immunity. 2011 Mar 30. PMID:21458306<ref>PMID:21458306</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3qrf" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 29: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bandukwala, H S]]
+[[Category: Bandukwala HS]]
-[[Category: Barbosa, B]]
+[[Category: Barbosa B]]
-[[Category: Benoist, C]]
+[[Category: Benoist C]]
-[[Category: Chen, L]]
+[[Category: Chen L]]
-[[Category: Chen, Y]]
+[[Category: Chen Y]]
-[[Category: Feurer, M]]
+[[Category: Feurer M]]
-[[Category: Ghosh, S]]
+[[Category: Ghosh S]]
-[[Category: Mathis, D]]
+[[Category: Mathis D]]
-[[Category: Rao, A]]
+[[Category: Rao A]]
-[[Category: Stroud, J C]]
+[[Category: Stroud JC]]
-[[Category: Wu, Y]]
+[[Category: Wu Y]]
-[[Category: Beta barrel]]
-[[Category: Dna binding]]
-[[Category: Dna binding protein-dna complex]]
-[[Category: Domain swap]]
-[[Category: Double helix]]
-[[Category: Forkhead domain]]
-[[Category: Immnoglobulin fold]]
-[[Category: Nucleus]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription regulation]]

3qrf

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Structure of a domain-swapped FOXP3 dimer

Structural highlights

Function

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