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| - | [[Image:2jz1.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2jz1| PDB=2jz1 | SCENE= }} | | {{STRUCTURE_2jz1| PDB=2jz1 | SCENE= }} |
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| - | '''DSX_long'''
| + | ===DSX_long=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_18184648}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18184648 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18184648}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2JZ1 is a [[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=2JZ1 OCA]. | + | 2JZ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZ1 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Transcription]] | | [[Category: Transcription]] |
| | [[Category: Ubiquitin]] | | [[Category: Ubiquitin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 9 14:40:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:48:12 2008'' |
Revision as of 10:48, 29 July 2008
Template:STRUCTURE 2jz1
DSX_long
Template:ABSTRACT PUBMED 18184648
About this Structure
2JZ1 is a Single protein structure of sequence from Drosophila melanogaster. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 29 13:48:12 2008
