Mesh ： Amino Acid Motifs Amino Acid Sequence Animals Anopheles Circular Dichroism Cross-Linking Reagents / pharmacology Crystallography, X-Ray DNA / chemistry Databases as Topic Dimerization Drosophila / metabolism Drosophila Proteins / chemistry Drosophila melanogaster Insecta Light Models, Molecular Molecular Sequence Data Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Scattering, Radiation Sequence Homology, Amino Acid Time Factors Transcription Factors / chemistry Transcription, Genetic Zinc / chemistry Zinc Fingers

来  源：   DOI：10.1016/j.str.2003.09.015   PDF(Sci-hub)

Abstract：
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.
摘要：
果蝇的300多个C2H2锌指蛋白中约有三分之一含有保守序列基序，锌指相关结构域(ZAD)。编码ZAD蛋白的基因对昆虫的基因组具有特异性并在其中扩展。仅建立了三个ZAD编码基因功能，ZAD的作用是未知的。在这里，我们介绍了Grauzone（ZAD（Grau））的ZAD的晶体结构，一种果蝇转录因子，特异性控制母体Cdc20样APC亚基皮质。ZAD形成非典型的高音一样的锌配位褶皱。晶体中两个ZAD（Grau）分子的头尾排列表明二聚体形成，由交联和动态光散射支持的观察。结果表明，ZAD提供了一种新型的蛋白质-蛋白质相互作用模块，该模块表征了昆虫转录因子的大家族。
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