1lpv
From Proteopedia
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|PDB= 1lpv |SIZE=350|CAPTION= <scene name='initialview01'>1lpv</scene> | |PDB= 1lpv |SIZE=350|CAPTION= <scene name='initialview01'>1lpv</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpv OCA], [http://www.ebi.ac.uk/pdbsum/1lpv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lpv RCSB]</span> | ||
}} | }} | ||
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[[Category: Wilken, J.]] | [[Category: Wilken, J.]] | ||
[[Category: Zhu, L.]] | [[Category: Zhu, L.]] | ||
| - | [[Category: ZN]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
[[Category: drosophila melanogaster]] | [[Category: drosophila melanogaster]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:51 2008'' |
Revision as of 19:05, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
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