1zv1
From Proteopedia
(New page: 200px<br /><applet load="1zv1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zv1, resolution 1.60Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1zv1.gif|left|200px]]<br /><applet load="1zv1" size=" | + | [[Image:1zv1.gif|left|200px]]<br /><applet load="1zv1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zv1, resolution 1.60Å" /> | caption="1zv1, resolution 1.60Å" /> | ||
'''Crystal structure of the dimerization domain of doublesex protein from D. melanogaster'''<br /> | '''Crystal structure of the dimerization domain of doublesex protein from D. melanogaster'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Male- and female-specific isoforms of the Doublesex (DSX) transcription | + | Male- and female-specific isoforms of the Doublesex (DSX) transcription factor regulate somatic sexual differentiation in Drosophila. The isoforms (DSX(M) and DSX(F)) share an N-terminal DNA binding domain (the DM motif), broadly conserved among metazoan sex-determining pathways. DM-DNA recognition is enhanced by a C-terminal dimerization domain. The crystal structure of this domain, determined at a resolution of 1.6 A, reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. Although this alpha-helical motif is well characterized in pathways of DNA repair and subcellular trafficking, to our knowledge this is its first report in a transcription factor. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative ubiquitin binding surface. Key side chains at this interface, identified by alanine scanning mutagenesis, are conserved among DSX homologs. The mechanism of dimerization is thus unrelated to the low affinity domain swapping observed among ubiquitin-associated CUE domains. The unexpected observation of a ubiquitin-associated fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors. The possibility that the ubiquitination machinery participates in the regulation of sexual dimorphism is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZV1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | + | 1ZV1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZV1 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bayrer, J | + | [[Category: Bayrer, J R.]] |
[[Category: Li, B.]] | [[Category: Li, B.]] | ||
| - | [[Category: Phillips, N | + | [[Category: Phillips, N B.]] |
[[Category: Wan, Z.]] | [[Category: Wan, Z.]] | ||
| - | [[Category: Weiss, M | + | [[Category: Weiss, M A.]] |
[[Category: dimerization]] | [[Category: dimerization]] | ||
[[Category: doublesex]] | [[Category: doublesex]] | ||
| Line 24: | Line 24: | ||
[[Category: uba domain]] | [[Category: uba domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:21 2008'' |
Revision as of 14:19, 21 February 2008
|
Crystal structure of the dimerization domain of doublesex protein from D. melanogaster
Overview
Male- and female-specific isoforms of the Doublesex (DSX) transcription factor regulate somatic sexual differentiation in Drosophila. The isoforms (DSX(M) and DSX(F)) share an N-terminal DNA binding domain (the DM motif), broadly conserved among metazoan sex-determining pathways. DM-DNA recognition is enhanced by a C-terminal dimerization domain. The crystal structure of this domain, determined at a resolution of 1.6 A, reveals a novel dimeric arrangement of ubiquitin-associated (UBA) folds. Although this alpha-helical motif is well characterized in pathways of DNA repair and subcellular trafficking, to our knowledge this is its first report in a transcription factor. Dimerization is mediated by a non-canonical hydrophobic interface extrinsic to the putative ubiquitin binding surface. Key side chains at this interface, identified by alanine scanning mutagenesis, are conserved among DSX homologs. The mechanism of dimerization is thus unrelated to the low affinity domain swapping observed among ubiquitin-associated CUE domains. The unexpected observation of a ubiquitin-associated fold in DSX extends the repertoire of alpha-helical dimerization elements in transcription factors. The possibility that the ubiquitination machinery participates in the regulation of sexual dimorphism is discussed.
About this Structure
1ZV1 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Dimerization of doublesex is mediated by a cryptic ubiquitin-associated domain fold: implications for sex-specific gene regulation., Bayrer JR, Zhang W, Weiss MA, J Biol Chem. 2005 Sep 23;280(38):32989-96. Epub 2005 Jul 27. PMID:16049008
Page seeded by OCA on Thu Feb 21 16:19:21 2008
