The 2.8 Å crystal structure of visual arrestin:: A model for arrestin's regulation
The 2.8 Å crystal structure of visual arrestin:: A model for arrestin's regulation
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DOI：
10.1016/s0092-8674(00)80735-7
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发表时间：
1999-04-16
期刊：
影响因子：
64.5
通讯作者：
Sigler, PB
中科院分区：
文献类型：
--
作者：
Hirsch, JA;Schubert, C;Sigler, PB
G 蛋白偶联信号传导被多种真核生物用来传递来自细胞外环境的信息。信号终止是通过抑制蛋白的作用实现的，抑制蛋白与激活的磷酸化 G 蛋白偶联受体结合。我们在此描述视觉视紫红质抑制蛋白基本构象的晶体学研究。该结构的显着特征是具有不寻常极性核心的二分分子。该核心部分通过延长的羧基末端尾部来稳定，该尾部将分子锁定在非活性状态。此外，发现视紫红质抑制蛋白是两个不对称分子的二聚体，表明其具有内在的构象可塑性。结合生化和诱变数据，我们提出了抑制蛋白被激活以与受体结合的分子机制。
G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding.