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==Structure of a domain-swapped FOXP3 dimer==
==Structure of a domain-swapped FOXP3 dimer==
<StructureSection load='3qrf' size='340' side='right' caption='[[3qrf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3qrf' size='340' side='right'caption='[[3qrf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qrf]] is a 10 chain structure with sequence 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=3QRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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"><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">[[1a02|1a02]], [[1owr|1owr]], [[2as5|2as5]], [[2a07|2a07]]</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), FOXP3, IPEX, JM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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>
<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=3qrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qrf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qrf RCSB], [http://www.ebi.ac.uk/pdbsum/3qrf PDBsum]</span></td></tr>
</table>
</table>
== Disease ==
[[http://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 ==
== Function ==
[[http://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>  [[http://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>


==See Also==
==See Also==
*[[Forkhead Box Protein 3|Forkhead Box Protein 3]]
*[[FOX 3D structures|FOX 3D structures]]
*[[Forkhead box protein|Forkhead box protein]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bandukwala, H S]]
[[Category: Large Structures]]
[[Category: Barbosa, B]]
[[Category: Bandukwala HS]]
[[Category: Benoist, C]]
[[Category: Barbosa B]]
[[Category: Chen, L]]
[[Category: Benoist C]]
[[Category: Chen, Y]]
[[Category: Chen L]]
[[Category: Feurer, M]]
[[Category: Chen Y]]
[[Category: Ghosh, S]]
[[Category: Feurer M]]
[[Category: Mathis, D]]
[[Category: Ghosh S]]
[[Category: Rao, A]]
[[Category: Mathis D]]
[[Category: Stroud, J C]]
[[Category: Rao A]]
[[Category: Wu, Y]]
[[Category: Stroud JC]]
[[Category: Beta barrel]]
[[Category: Wu Y]]
[[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]]

Latest revision as of 14:55, 14 March 2024

Structure of a domain-swapped FOXP3 dimerStructure of a domain-swapped FOXP3 dimer

Structural highlights

3qrf is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

See Also

References

  1. ↑ Yiu GK, Kaunisto A, Chin YR, Toker A. NFAT promotes carcinoma invasive migration through glypican-6. Biochem J. 2011 Nov 15;440(1):157-66. doi: 10.1042/BJ20110530. PMID:21871017 doi:10.1042/BJ20110530

3qrf, resolution 2.80Å

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