1zv1

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{{STRUCTURE_1zv1| PDB=1zv1 | SCENE= }}
{{STRUCTURE_1zv1| PDB=1zv1 | SCENE= }}
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'''Crystal structure of the dimerization domain of doublesex protein from D. melanogaster'''
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===Crystal structure of the dimerization domain of doublesex protein from D. melanogaster===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16049008 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16049008}}
==About this Structure==
==About this Structure==
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[[Category: Transcription factor]]
[[Category: Transcription factor]]
[[Category: Uba domain]]
[[Category: Uba domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:06:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:24:59 2008''

Revision as of 20:25, 27 July 2008

Image:1zv1.png

Template:STRUCTURE 1zv1

Crystal structure of the dimerization domain of doublesex protein from D. melanogaster

Template:ABSTRACT PUBMED 16049008

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

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