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首页> 外文期刊>Biological chemistry >Characterization of the Ligand-Binding Domain of the Ecdysteroid Receptor from Drosophila Melanogaster
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Characterization of the Ligand-Binding Domain of the Ecdysteroid Receptor from Drosophila Melanogaster

机译：果蝇蜕皮甾体受体的配体结合域的表征。

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Mutants created by site-directed mutagenesis were used to elucidate the function of amino acids involved in ligand binding to ecdysteroid receptor (EcR) and heterodimer formation with ultraspiracle (USP). The results demonstrate the importance of the C-terminal part of the D-domain and helix 12 of EcR for hormone binding. Some amino acids are involved either in ligand binding to EcR (E476, M504, D572, I617, N626) or ligand-dependent heterodimerization as determined by gel mobility shift assays (A612, L615, T619), while others are involved in both functions (K497, E648). Some amino acids are suboptimal for ligand binding (L615, T619), but mediate ligand-dependent dimerization. We conclude that the enhanced regulatory potential by ligand-dependent modulation of dimerization in the wild type is achieved at the expense of optimal ligand binding. Mutation of amino acids (K497, E648) involved in the salt bridge between helix 4 and 12 impair ligand binding to EcR more severely than hormone binding to the heterodimer, indicating that to some extent heterodimerization compensates for the deleterious effect of certain mutations. Different effects of the same point mutations on ligand binding to EcR and EcR/USP (R511, A612, L615, I617, T619, N626) indicate that the ligand-binding pocket is modified by heterodimerization.
机译：通过定点诱变产生的突变体用于阐明参与配体与蜕皮甾类受体（EcR）结合的氨基酸的功能，以及与超螺旋体形成异二聚体（USP）的功能。结果证明，Dc结构域的C末端部分和EcR的螺旋12对于激素结合非常重要。一些氨基酸要么参与配体与EcR的结合（E476，M504，D572，I617，N626），要么通过凝胶迁移率变动分析（A612，L615，T619）确定与配体有关的异二聚体，而其他氨基酸则同时参与这两种功能（ K497，E648）。一些氨基酸对于配体结合而言不是最理想的（L615，T619），但介导配体依赖性二聚作用。我们得出结论，在野生型中通过配体依赖性的二聚化调节增强了调节潜力，但以最佳的配体结合为代价。螺旋4和12之间的盐桥中涉及的氨基酸（K497，E648）突变比与异源二聚体的激素结合更严重地削弱了配体与EcR的结合，表明异源二聚化在一定程度上补偿了某些突变的有害作用。相同点突变对配体与EcR和EcR / USP结合的不同作用（R511，A612，L615，I617，T619，N626）表明，配体结合口袋被异二聚化修饰。

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