1pzw
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(New page: 200px<br /><applet load="1pzw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pzw, resolution 2.00Å" /> '''Crystal structure of...)
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Revision as of 22:08, 20 November 2007
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Crystal structure of the zinc finger associated domain of the Drosophila transcription factor Grauzone
Overview
About one-third of the more than 300 C2H2 zinc finger proteins of, Drosophila contain a conserved sequence motif, the zinc finger-associated, domain (ZAD). Genes that encode ZAD proteins are specific for and expanded, in the genomes of insects. Only three ZAD-encoding gene functions are, established, and the role of ZAD is unknown. Here we present the crystal, structure of the ZAD of Grauzone (ZAD(Grau)), a Drosophila transcription, factor that specifically controls the maternal Cdc20-like APC subunit, Cortex. ZAD forms an atypical treble-clef-like zinc-coordinating fold., Head-to-tail arrangement of two ZAD(Grau) molecules in the crystals, suggests dimer formation, an observation supported by crosslinking and, dynamic light scattering. The results indicate that ZAD provides a novel, protein-protein interaction module that characterizes a large family of, insect transcription factors.
About this Structure
1PZW is a Single protein structure of sequence from Drosophila melanogaster with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The zinc finger-associated domain of the Drosophila transcription factor grauzone is a novel zinc-coordinating protein-protein interaction module., Jauch R, Bourenkov GP, Chung HR, Urlaub H, Reidt U, Jackle H, Wahl MC, Structure. 2003 Nov;11(11):1393-402. PMID:14604529
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