4wk8
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==FOXP3 forms a domain-swapped dimer to bridge DNA== |
+ | <StructureSection load='4wk8' size='340' side='right' caption='[[4wk8]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4wk8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WK8 FirstGlance]. <br> | ||
+ | </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=4wk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wk8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wk8 RCSB], [http://www.ebi.ac.uk/pdbsum/4wk8 PDBsum]</span></td></tr> | ||
+ | </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 == | ||
+ | [[http://www.uniprot.org/uniprot/FOXP3_HUMAN FOXP3_HUMAN]] Probable transcription factor. Plays a critical role in the control of immune response. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | FOXP3 is a lineage-specific transcription factor that is required for regulatory T cell development and function. In this study, we determined the crystal structure of the FOXP3 forkhead domain bound to DNA. The structure reveals that FOXP3 can form a stable domain-swapped dimer to bridge DNA in the absence of cofactors, suggesting that FOXP3 may play a role in long-range gene interactions. To test this hypothesis, we used circular chromosome conformation capture coupled with high throughput sequencing (4C-seq) to analyze FOXP3-dependent genomic contacts around a known FOXP3-bound locus, Ptpn22. Our studies reveal that FOXP3 induces significant changes in the chromatin contacts between the Ptpn22 locus and other Foxp3-regulated genes, reflecting a mechanism by which FOXP3 reorganizes the genome architecture to coordinate the expression of its target genes. Our results suggest that FOXP3 mediates long-range chromatin interactions as part of its mechanisms to regulate specific gene expression in regulatory T cells. | ||
- | + | DNA binding by FOXP3 domain-swapped dimer suggests mechanisms of long-range chromosomal interactions.,Chen Y, Chen C, Zhang Z, Liu CC, Johnson ME, Espinoza CA, Edsall LE, Ren B, Zhou XJ, Grant SF, Wells AD, Chen L Nucleic Acids Res. 2015 Jan 7. pii: gku1373. PMID:25567984<ref>PMID:25567984</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Chen, L]] | ||
[[Category: Chen, Y]] | [[Category: Chen, Y]] | ||
- | [[Category: | + | [[Category: Dna bridging]] |
+ | [[Category: Foxp3]] | ||
+ | [[Category: Regulatory t cell]] | ||
+ | [[Category: Transcription regulation]] |
Revision as of 16:47, 21 January 2015
FOXP3 forms a domain-swapped dimer to bridge DNA
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