1lpv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lpv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lpv" /> '''DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR...)
Line 1: Line 1:
-
[[Image:1lpv.jpg|left|200px]]<br /><applet load="1lpv" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1lpv.jpg|left|200px]]<br /><applet load="1lpv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lpv" />
caption="1lpv" />
'''DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES'''<br />
'''DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES'''<br />
==Overview==
==Overview==
-
Sex determination is regulated by diverse pathways. Although upstream, signals vary, a cysteine-rich DNA-binding domain (the DM motif) is, conserved within downstream transcription factors of Drosophila, melanogaster (Doublesex) and Caenorhabditis elegans (MAB-3). Vertebrate DM, genes have likewise been identified and, remarkably, are associated with, human sex reversal (46, XY gonadal dysgenesis). Here we demonstrate that, the structure of the Doublesex domain contains a novel zinc module and, disordered tail. The module consists of intertwined CCHC and HCCC, Zn(2+)-binding sites; the tail functions as a nascent recognition, alpha-helix. Mutations in either Zn(2+)-binding site or tail can lead to, an intersex phenotype. The motif binds in the DNA minor groove without, sharp DNA bending. These molecular features, unusual among zinc fingers, and zinc modules, underlie the organization of a Drosophila enhancer that, integrates sex- and tissue-specific signals. The structure provides a, foundation for analysis of DM mutations affecting sexual dimorphism and, courtship behavior.
+
Sex determination is regulated by diverse pathways. Although upstream signals vary, a cysteine-rich DNA-binding domain (the DM motif) is conserved within downstream transcription factors of Drosophila melanogaster (Doublesex) and Caenorhabditis elegans (MAB-3). Vertebrate DM genes have likewise been identified and, remarkably, are associated with human sex reversal (46, XY gonadal dysgenesis). Here we demonstrate that the structure of the Doublesex domain contains a novel zinc module and disordered tail. The module consists of intertwined CCHC and HCCC Zn(2+)-binding sites; the tail functions as a nascent recognition alpha-helix. Mutations in either Zn(2+)-binding site or tail can lead to an intersex phenotype. The motif binds in the DNA minor groove without sharp DNA bending. These molecular features, unusual among zinc fingers and zinc modules, underlie the organization of a Drosophila enhancer that integrates sex- and tissue-specific signals. The structure provides a foundation for analysis of DM mutations affecting sexual dimorphism and courtship behavior.
==About this Structure==
==About this Structure==
-
1LPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LPV OCA].
+
1LPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPV OCA].
==Reference==
==Reference==
Line 17: Line 17:
[[Category: Phillips, N.]]
[[Category: Phillips, N.]]
[[Category: Stratton, S.]]
[[Category: Stratton, S.]]
-
[[Category: Weiss, M.A.]]
+
[[Category: Weiss, M A.]]
[[Category: Wilken, J.]]
[[Category: Wilken, J.]]
[[Category: Zhu, L.]]
[[Category: Zhu, L.]]
Line 27: Line 27:
[[Category: transcription]]
[[Category: transcription]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:46:20 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:14 2008''

Revision as of 11:47, 21 February 2008

Image:1lpv.jpg

1lpv

Drag the structure with the mouse to rotate

DROSOPHILA MELANOGASTER DOUBLESEX (DSX), NMR, 18 STRUCTURES

Overview

Sex determination is regulated by diverse pathways. Although upstream signals vary, a cysteine-rich DNA-binding domain (the DM motif) is conserved within downstream transcription factors of Drosophila melanogaster (Doublesex) and Caenorhabditis elegans (MAB-3). Vertebrate DM genes have likewise been identified and, remarkably, are associated with human sex reversal (46, XY gonadal dysgenesis). Here we demonstrate that the structure of the Doublesex domain contains a novel zinc module and disordered tail. The module consists of intertwined CCHC and HCCC Zn(2+)-binding sites; the tail functions as a nascent recognition alpha-helix. Mutations in either Zn(2+)-binding site or tail can lead to an intersex phenotype. The motif binds in the DNA minor groove without sharp DNA bending. These molecular features, unusual among zinc fingers and zinc modules, underlie the organization of a Drosophila enhancer that integrates sex- and tissue-specific signals. The structure provides a foundation for analysis of DM mutations affecting sexual dimorphism and courtship behavior.

About this Structure

1LPV is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Sexual dimorphism in diverse metazoans is regulated by a novel class of intertwined zinc fingers., Zhu L, Wilken J, Phillips NB, Narendra U, Chan G, Stratton SM, Kent SB, Weiss MA, Genes Dev. 2000 Jul 15;14(14):1750-64. PMID:10898790

Page seeded by OCA on Thu Feb 21 13:47:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lpv"
Personal tools