4wk8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
==FOXP3 forms a domain-swapped dimer to bridge DNA==
 +
<StructureSection load='4wk8' size='340' side='right' caption='[[4wk8]], [[Resolution|resolution]] 3.40&Aring;' 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.
-
The entry 4wk8 is ON HOLD until Paper Publication
+
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>
-
Authors: Chen, Y., Chen, L.
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
Description: FOXP3 forms a domain-swapped dimer to bridge DNA
+
== References ==
-
[[Category: Unreleased Structures]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Chen, L]]
[[Category: Chen, Y]]
[[Category: Chen, Y]]
-
[[Category: Chen, L]]
+
[[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

4wk8, resolution 3.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools