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| | ==DSX_short== | | ==DSX_short== |
| - | <StructureSection load='2jz0' size='340' side='right' caption='[[2jz0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jz0' size='340' side='right'caption='[[2jz0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jz0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JZ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jz0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JZ0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jz1|2jz1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=2jz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jz0 OCA], [https://pdbe.org/2jz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2jz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jz0 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=2jz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jz0 OCA], [http://pdbe.org/2jz0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jz0 RCSB], [http://www.ebi.ac.uk/pdbsum/2jz0 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DSX_DROME DSX_DROME]] Controls somatic sexual differentiation. Binds directly and specifically to the FBE (fat body enhancer) of the yolk protein 1 and 2 genes (Yp1 and Yp2). This enhancer is sufficient to direct the female-specific transcription characteristic of the Yp genes in adult fat bodies. Involved in regulation of male-specific expression of takeout in brain-associated fat body.<ref>PMID:12435630</ref> | + | [https://www.uniprot.org/uniprot/DSX_DROME DSX_DROME] Controls somatic sexual differentiation. Binds directly and specifically to the FBE (fat body enhancer) of the yolk protein 1 and 2 genes (Yp1 and Yp2). This enhancer is sufficient to direct the female-specific transcription characteristic of the Yp genes in adult fat bodies. Involved in regulation of male-specific expression of takeout in brain-associated fat body.<ref>PMID:12435630</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jz0_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/2jz0_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Bayrer, J R]] | + | [[Category: Large Structures]] |
| - | [[Category: Weiss, M A]] | + | [[Category: Bayrer JR]] |
| - | [[Category: Yang, Y]] | + | [[Category: Weiss MA]] |
| - | [[Category: Zhang, W]] | + | [[Category: Yang Y]] |
| - | [[Category: Development]] | + | [[Category: Zhang W]] |
| - | [[Category: Double sex]]
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| - | [[Category: Gene regulation]]
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| - | [[Category: Sex determination]]
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| - | [[Category: Transcription]]
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| - | [[Category: Ubiquitin]]
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| Structural highlights
Function
DSX_DROME Controls somatic sexual differentiation. Binds directly and specifically to the FBE (fat body enhancer) of the yolk protein 1 and 2 genes (Yp1 and Yp2). This enhancer is sufficient to direct the female-specific transcription characteristic of the Yp genes in adult fat bodies. Involved in regulation of male-specific expression of takeout in brain-associated fat body.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The DSX (Doublesex) transcription factor regulates somatic sexual differentiation in Drosophila. Female and male isoforms (DSX F and DSX M) are formed due to sex-specific RNA splicing. DNA recognition, mediated by a shared N-terminal zinc module (the DM domain), is enhanced by a C-terminal dimerization element. Sex-specific extension of this element in DSX F and DSX M leads to assembly of distinct transcriptional preinitiation complexes. Here, we describe the structure of the extended C-terminal dimerization domain of DSX F as determined by multidimensional NMR spectroscopy. The core dimerization element is well ordered, giving rise to a dense network of interresidue nuclear Overhauser enhancements. The structure contains dimer-related UBA folds similar to those defined by x-ray crystallographic studies of a truncated domain. Whereas the proximal portion of the female tail extends helix 3 of the UBA fold, the distal tail is disordered. Ala substitutions in the proximal tail disrupt the sex-specific binding of IX (Intersex), an obligatory partner protein and putative transcriptional coactivator; IX-DSX F interaction is, by contrast, not disrupted by truncation of the distal tail. Mutagenesis of the UBA-like dimer of DSX F highlights the importance of steric and electrostatic complementarity across the interface. Two temperature-sensitive mutations at this interface have been characterized in yeast model systems. One weakens a network of solvated salt bridges, whereas the other perturbs the underlying nonpolar interface. These mutations confer graded gene-regulatory activity in yeast within a physiological temperature range and so may provide novel probes for genetic analysis of a sex-specific transcriptional program in Drosophila development.
Doublesex and the regulation of sexual dimorphism in Drosophila melanogaster: structure, function, and mutagenesis of a female-specific domain.,Yang Y, Zhang W, Bayrer JR, Weiss MA J Biol Chem. 2008 Mar 14;283(11):7280-92. Epub 2008 Jan 9. PMID:18184648[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dauwalder B, Tsujimoto S, Moss J, Mattox W. The Drosophila takeout gene is regulated by the somatic sex-determination pathway and affects male courtship behavior. Genes Dev. 2002 Nov 15;16(22):2879-92. PMID:12435630 doi:http://dx.doi.org/10.1101/gad.1010302
- ↑ Yang Y, Zhang W, Bayrer JR, Weiss MA. Doublesex and the regulation of sexual dimorphism in Drosophila melanogaster: structure, function, and mutagenesis of a female-specific domain. J Biol Chem. 2008 Mar 14;283(11):7280-92. Epub 2008 Jan 9. PMID:18184648 doi:10.1074/jbc.M708742200
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